The Sec System: Protein Export in Escherichia coli

scientific article published in November 2017

The Sec System: Protein Export in Escherichia coli is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/ECOSALPLUS.ESP-0002-2017
P932PMC publication ID5807066
P698PubMed publication ID29165233

P2093author name stringLinda L Randall
Jennine M Crane
P2860cites workA highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecBQ73138769
The high affinity ATP binding site modulates the SecA-precursor interactionQ73276020
Evidence that SecB enhances the activity of SecAQ73738765
Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactionsQ73783901
A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secBQ73905825
Expression of gpsA encoding biosynthetic sn-glycerol 3-phosphate dehydrogenase suppresses both the LB- phenotype of a secB null mutant and the cold-sensitive phenotype of a secG null mutantQ74027915
The phase property of membrane phospholipids is affected by the functionality of signal peptides from the Escherichia coli ribose-binding proteinQ74066173
YidC mediates membrane protein insertion in bacteriaQ74191988
SecA folds via a dimeric intermediateQ74337250
Tyr-326 plays a critical role in controlling SecA-preprotein interactionQ74347195
PROTEIN SYNTHESIS BY POLYRIBOSOMES ON PROTOPLAST MEMBRANES OF B. MEGATERIUMQ76606257
ON THE CYTOLOGICAL UNIT FOR PROTEIN SYNTHESIS IN VIVO IN E. COLI. II. STUDIES WITH INTACT CELLS OF TYPE BQ76850072
Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimersQ77927053
A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecAQ80310735
Determining the conductance of the SecY protein translocation channel for small moleculesQ80390141
Structure of the E. coli protein-conducting channel bound to a translating ribosomeQ24539141
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationQ24596484
Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecBQ24618046
Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequencesQ24644640
Preprotein-controlled catalysis in the helicase motor of SecAQ24670723
Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myelomaQ24681545
Assembly and structure of the T3SSQ26865556
A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and functionQ26995227
Structure and mechanism of Escherichia coli type I signal peptidaseQ26999911
YidC/Alb3/Oxa1 Family of InsertasesQ27025116
Crystal structure of the bacterial protein export chaperone secBQ27628763
Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschiiQ27629461
Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanismQ27636769
Nucleotide control of interdomain interactions in the conformational reaction cycle of SecAQ27639672
Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPaseQ27640590
Structural determinants of SecB recognition by SecA in bacterial protein translocationQ27642253
Crystal structure of SecB from Escherichia coliQ27642641
X-ray structure of a protein-conducting channelQ27642744
Structure of dimeric SecA, the Escherichia coli preprotein translocase motorQ27643567
Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMRQ27649095
Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twistQ27649284
Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidCQ27649371
Ribosome binding of a single copy of the SecY complex: implications for protein translocationQ27649425
Crystal structure of a bacterial signal Peptide peptidaseQ27649465
The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleftQ27649739
Analysis of the isolated SecA DEAD motor suggests a mechanism for chemical-mechanical couplingQ27651892
Structure of a complex of the ATPase SecA and the protein-translocation channelQ27652526
Conformational transition of Sec machinery inferred from bacterial SecYE structuresQ27652527
Crystallographic analysis of bacterial signal peptidase in ternary complex with arylomycin A2 and a beta-sultam inhibitorQ27656899
Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecAQ27657911
Regulation of the Protein-Conducting Channel by a Bound RibosomeQ27658163
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranesQ27664605
Cryo-EM structure of the ribosome–SecYE complex in the membrane environmentQ27667539
Protein transport by the bacterial Tat pathwayQ38192369
Architecture and assembly of the Type VI secretion system.Q38200408
The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Q38206834
Fidelity of cotranslational protein targeting by the signal recognition particleQ38217500
Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB.Q38291165
Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPaseQ38314889
SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coliQ38322783
A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.Q38336960
Characterization of a region in mature LamB protein that interacts with a component of the export machinery of Escherichia coliQ38338625
Escherichia coli sec mutants accumulate a processed immature form of maltose-binding protein (MBP), a late-phase intermediate in MBP exportQ38338914
Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli.Q38341113
The antifolding activity of SecB promotes the export of the E. coli maltose-binding proteinQ38347439
Diverse effects of the MalE-LacZ hybrid protein on Escherichia coli cell physiologyQ38350783
E. coli mutant pleiotropically defective in the export of secreted proteinsQ38356083
Different exported proteins in E. coli show differences in the temporal mode of processing in vivoQ38356214
Protein localization in E. coli: is there a common step in the secretion of periplasmic and outer-membrane proteins?Q38356265
Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasmQ38357752
Molecular chaperones: proteins essential for the biogenesis of some macromolecular structuresQ38365596
Viability of an Escherichia coli pgsA null mutant lacking detectable phosphatidylglycerol and cardiolipinQ39498543
The SecA subunit of Escherichia coli preprotein translocase is exposed to the periplasmQ39568449
Genetic studies on protein export in bacteriaQ39590426
Folded HasA inhibits its own secretion through its ABC exporterQ39645637
Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membraneQ39647998
The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporterQ39702705
Influence of impaired chaperone or secretion function on SecB production in Escherichia coliQ39843192
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocaseQ39918354
SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membraneQ39932560
Involvement of SecB, a chaperone, in the export of ribose-binding proteinQ39935707
Conformational dynamics of the plug domain of the SecYEG protein-conducting channel.Q39935945
Determinants of the quantity of the stable SecY complex in the Escherichia coli cellQ39938069
Regulation of the Escherichia coli secA gene by protein secretion defects: analysis of secA, secB, secD, and secY mutantsQ39953808
Transcriptional organization within an Escherichia coli cell division gene cluster: direction of transcription of the cell separation gene envAQ39966114
Multiple SecA molecules drive protein translocation across a single translocon with SecG inversionQ40082687
Mechanism of incorporation of cell envelope proteins in Escherichia coliQ40248345
BINDING OF RIBOSOMES TO CYTOPLASMIC RETICULUM OF BACILLUS MEGATERIUM.Q40438491
A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli.Q40456503
A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidaseQ34346496
Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyadQ34356733
Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile.Q34363960
Structural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy.Q34442682
MPIase is a glycolipozyme essential for membrane protein integrationQ34509067
Elongation arrest by SecM via a cascade of ribosomal RNA rearrangementsQ34528562
How azide inhibits ATP hydrolysis by the F-ATPases.Q34637621
YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocaseQ34663216
Energetics of SecA dimerizationQ34761920
Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical moleculesQ34977908
Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitroQ35018606
SecB, one small chaperone in the complex milieu of the cellQ35021874
Extracellular labeling of nascent polypeptides traversing the membrane of Escherichia coliQ35035545
Conformational variation of the translocon enhancing chaperone SecDF.Q35076035
The translational regulatory function of SecM requires the precise timing of membrane targeting.Q35098853
Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteriaQ35170737
The basis of asymmetry in the SecA:SecB complexQ35207949
Subunit dynamics in Escherichia coli preprotein translocaseQ35271076
Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB.Q35582444
Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioningQ35587373
A single copy of SecYEG is sufficient for preprotein translocationQ35591711
Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesiclesQ35610508
Escherichia coli SecB stimulates export without maintaining export competence of ribose-binding protein signal sequence mutants.Q35614280
Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranesQ35619782
Control of SecA and SecM translation by protein secretionQ35737959
Selective photoaffinity labeling identifies the signal peptide binding domain on SecAQ35750297
Conformational Changes of the Clamp of the Protein Translocation ATPase SecAQ35754823
The bacterial Sec-translocase: structure and mechanism.Q35814696
Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPaseQ35837206
Heat-shock proteins can substitute for SecB function during protein export in Escherichia coliQ35920818
Position-dependent effects of polylysine on Sec protein transportQ35921553
One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.Q35926815
Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteinsQ35962797
PrlA and PrlG suppressors reduce the requirement for signal sequence recognitionQ35975083
Structure and function of a membrane component SecDF that enhances protein exportQ27667802
Synthesis and Characterization of the Arylomycin Lipoglycopeptide Antibiotics and the Crystallographic Analysis of Their Complex with Signal PeptidaseQ27675041
ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA TranslocaseQ27675185
Structure of the SecY channel during initiation of protein translocationQ27680440
A structural model of the active ribosome-bound membrane protein insertase YidCQ27684647
Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound StateQ27702712
Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitorQ27766053
Effects of pre-protein overexpression on SecB synthesis in Escherichia coliQ28140412
Three-dimensional structure of the bacterial protein-translocation complex SecYEGQ28217206
Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitroQ28264700
Modulation of folding pathways of exported proteins by the leader sequenceQ28294571
Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coliQ28299991
Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA functionQ28354455
Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channelsQ28535409
SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificityQ28740702
Patterns of amino acids near signal-sequence cleavage sitesQ29616542
Outer membrane lipoprotein biogenesis: Lol is not the end.Q30152837
The Bam machine: a molecular cooperQ30155481
Lipoprotein sorting in bacteria.Q30155534
Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: evidence from site-directed mutagenesis and carbodiimide labelingQ30268386
Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli.Q30401105
SecA, the motor of the secretion machine, binds diverse partners on one interactive surfaceQ30485740
Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labelingQ30496200
Orientation of SecA and SecB in complex, derived from disulfide cross-linkingQ30497880
The oligomeric state and arrangement of the active bacterial transloconQ30498189
A large conformational change of the translocation ATPase SecAQ30776655
Substrate specificity of the SecB chaperoneQ30815173
A comprehensive database of verified experimental data on protein folding kineticsQ30852309
Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibriumQ31664450
Secretion monitor, SecM, undergoes self-translation arrest in the cytosolQ31923120
SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.Q33562009
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coliQ33562047
Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway.Q47611174
Effects of nonlamellar-prone lipids on the ATPase activity of SecA bound to model membranesQ47682273
Cell-Free Protein Synthesis: Effects of Age and State of Ribosomal AggregationQ47715200
Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranesQ47763987
Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles.Q47917595
Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerolQ48080100
Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelopeQ48395760
Evidence for posttranslational translocation of beta-lactamase across the bacterial inner membrane.Q50213210
Protein sizes and stoichiometry in the chaperone SecB--RBPTI complex estimated by ANS fluorescence.Q50524678
Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB.Q50759209
The long alpha-helix of SecA is important for the ATPase coupling of translocation.Q51127253
SecA protein is required for secretory protein translocation into E. coli membrane vesicles.Q52455868
Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane.Q52457501
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.Q52513940
Zinc stabilizes the SecB binding site of SecA.Q52534778
The role of the conserved box E residues in the active site of the Escherichia coli type I signal peptidase.Q52538173
Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.Q52563568
Measurement of intracellular sodium concentration and sodium transport in Escherichia coli by 23Na nuclear magnetic resonance.Q52645070
Characterization of the annular lipid shell of the Sec translocon.Q53446395
Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli.Q54154827
Reconstitution of functionally efficient SecA-dependent protein-conducting channels: transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels.Q54318600
In vitro analysis of the process of translocation of OmpA across the Escherichia coli cytoplasmic membrane. A translocation intermediate accumulates transiently in the absence of the proton motive force.Q54340916
Conformational changes of the chaperone SecB upon binding to a model substrate--bovine pancreatic trypsin inhibitor (BPTI).Q54354833
Expression, purification and characterization of the Escherichia coli integral membrane protein YajC.Q54372106
Systematic analysis of native membrane protein complexes in Escherichia coli.Q54372766
Expression and purification of the recombinant membrane protein YidC: a case study for increased stability and solubility.Q54420417
The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon.Q54423305
Topology inversion of SecG is essential for cytosolic SecA-dependent stimulation of protein translocation.Q54436102
Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel.Q54443529
Allosteric regulation of SecA: magnesium-mediated control of conformation and activity.Q54443615
Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity.Q54452792
Defining the role of the Escherichia coli chaperone SecB using comparative proteomics.Q54473734
NMR structure of the C-terminal domain of SecA in the free state.Q54497650
Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.Q54535975
Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR.Q54536175
SecDFyajC forms a heterotetrameric complex with YidC.Q54543620
Targeting, insertion, and localization of Escherichia coli YidC.Q54551389
Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding.Q54559159
Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands.Q54561671
Identification of a region of interaction between Escherichia coli SecA and SecY proteins.Q54567468
Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase.Q54567779
A significant fraction of functional SecA is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation.Q54576716
Different PrlA proteins increase the efficiency of periplasmic production of human interleukin-6 in Escherichia coli.Q54582761
SecG plays a critical role in protein translocation in the absence of the proton motive force as well as at low temperature.Q54593351
SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.Q54598039
Mapping of the Binding Frame for the Chaperone SecB within a Natural Ligand, Galactose-binding ProteinQ54601274
A quantitative assay to determine the amount of signal peptidase I in E. coli and the orientation of membrane vesicles.Q54602070
The C terminus of SecA is involved in both lipid binding and SecB binding.Q54614038
Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo.Q54633342
Membrane vesicles containing overproduced SecY and SecE exhibit high translocation ATPase activity and countermovement of protons in a SecA- and presecretory protein-dependent manner.Q54658915
Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivoQ36098016
Accumulation of secretory protein precursors in Escherichia coli induces the heat shock responseQ36102319
Genetic and molecular characterization of the Escherichia coli secD operon and its productsQ36105112
Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coliQ36123480
Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3Q36150427
Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Q36155063
Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operonQ36159495
The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitroQ36164926
The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export.Q36174105
Bacterial protein translocation requires only one copy of the SecY complex in vivoQ36205340
Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysisQ36215035
secD, a new gene involved in protein export in Escherichia coliQ36231634
Suppression of a signal sequence mutation by an amino acid substitution in the mature portion of the maltose-binding proteinQ36234894
Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coliQ36253218
Determination of the binding frame within a physiological ligand for the chaperone SecB.Q36278522
Interaction of SecB with intermediates along the folding pathway of maltose-binding proteinQ36279244
Electrospray mass spectrometric investigation of the chaperone SecB.Q36279705
Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding proteinQ36280530
The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for bindingQ36280717
Calorimetric analyses of the interaction between SecB and its ligandsQ36280993
Proper interaction between at least two components is required for efficient export of proteins to the Escherichia coli cell envelopeQ36289283
Post-translational modification and processing of Escherichia coli prolipoprotein in vitroQ36289591
Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY.Q36321596
Mutations in a new gene, secB, cause defective protein localization in Escherichia coliQ36326983
Evidence for specificity at an early step in protein export in Escherichia coliQ36361933
Role for membrane potential in the secretion of protein into the periplasm of Escherichia coliQ36366860
Isolation of the Escherichia coli leader peptidase gene and effects of leader peptidase overproduction in vivoQ36373675
Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coliQ36390365
Cation transport in Escherichia coli. VIII. Potassium transport mutantsQ36407638
Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complexQ36455887
Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Q36575070
Complex behavior in solution of homodimeric SecA.Q36639172
Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linkingQ36674746
High selectivity with low specificity: how SecB has solved the paradox of chaperone bindingQ40497588
Nucleotide and Phospholipid-Dependent Control of PPXD and C-Domain Association for SecA ATPaseQ40549080
A new form of structural lipoprotein of outer membrane of Escherichia coliQ40757311
Precursors of major outer membrane proteins of Escherichia coliQ40807978
Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coliQ40820187
The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.Q41006640
Induction of non-bilayer lipid structures by functional signal peptidesQ41204756
The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursorQ41219838
Synthesis of Exported Proteins by Membrane-Bound Polysomes from Escherichia coliQ41259974
DCCD inhibits protein translocation into plasma membrane vesicles from Escherichia coli at two different stepsQ41357977
Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linkingQ41445854
The requirement for energy during export of beta-lactamase in Escherichia coli is fulfilled by the total protonmotive forceQ41569479
Inactivation of protein translocation by cold-sensitive mutations in the yajC-secDF operonQ41820715
Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coliQ41827408
Requirements for substrate recognition by bacterial leader peptidaseQ41843667
The dynamic action of SecA during the initiation of protein translocation.Q41855262
Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligandsQ41866614
SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer studyQ41897858
Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein exportQ41904736
Protein synthesis by membrane-bound and free ribosomes of secretory and non-secretory tissuesQ41906977
Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteinsQ41960890
Structure of the SecY complex unlocked by a preprotein mimic.Q42000002
Tryptophan fluorescence study on the interaction of the signal peptide of the Escherichia coli outer membrane protein PhoE with model membranesQ42006855
Topologically fixed SecG is fully functionalQ42073427
Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecAQ42078600
YfgM is an ancillary subunit of the SecYEG translocon in Escherichia coliQ42087433
The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP releaseQ42152267
Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.Q42177840
Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocationQ42213460
Identification of the preprotein binding domain of SecA.Q42485674
Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer.Q42601546
The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane sealQ42621979
Prolyl-tRNA(Pro) in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA.Q42640310
Characterization of the Escherichia coli protein-export gene secB.Q42644465
Ion conductivity of the bacterial translocation channel SecYEG engaged in translocationQ42850306
The secD locus of E. coli codes for two membrane proteins required for protein exportQ42927284
Sites of interaction between SecA and the chaperone SecB, two proteins involved in exportQ43095210
A role for the two-helix finger of the SecA ATPase in protein translocation.Q43181763
Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB.Q43265896
Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coliQ43424522
SecB-mediated protein export need not occur via kinetic partitioningQ43527176
Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB.Q43660562
Differential expression of secretion machinery during bacterial growth: SecY and SecF decrease while SecA increases during transition from exponential phase to stationary phaseQ43661432
Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidaseQ43754168
SecDFyajC is not required for the maintenance of the proton motive forceQ43798449
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranesQ43822332
Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system.Q43895294
Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energizationQ43907653
Suppressor mutations that restore export of a protein with a defective signal sequenceQ43987617
Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA.Q44163723
Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrateQ44493487
Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interactionQ44560492
The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteinsQ44686930
Regulation of signal peptidase by phospholipids in membrane: characterization of phospholipid bilayer incorporated Escherichia coli signal peptidaseQ44713919
Alteration of the phospholipid composition of Escherichia coli through genetic manipulationQ44807226
Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitorQ44891154
Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational stateQ44925080
Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasmQ44976888
Solution NMR structure and X-ray absorption analysis of the C-terminal zinc-binding domain of the SecA ATPaseQ44983734
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.Q46008320
Effect of crowding agents, signal peptide, and chaperone SecB on the folding and aggregation of E. coli maltose binding protein.Q46055337
The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membraneQ46059428
ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocaseQ46481993
The oligomeric distribution of SecYEG is altered by SecA and translocation ligandsQ46768434
Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitroQ33577044
Mobility of cytoplasmic, membrane, and DNA-binding proteins in Escherichia coliQ33647888
Signal peptides are allosteric activators of the protein translocaseQ33662560
Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitroQ33678296
Identification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms.Q33723631
Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivoQ33726768
Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active transloconQ33737540
Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transferQ33773458
Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expressionQ33787527
SecM-stalled ribosomes adopt an altered geometry at the peptidyl transferase centerQ33803719
High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory proteinQ33820929
SecM facilitates translocase function of SecA by localizing its biosynthesisQ33848928
Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzymeQ33886664
The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cyclingQ33887254
The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter.Q33888292
PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocationQ33889035
The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunitsQ33891061
The secD locus of E.coli codes for two membrane proteins required for protein exportQ33922088
The action of cardiolipin on the bacterial translocon.Q33933121
A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant.Q33939397
A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene.Q33953915
Precursors of three exported proteins in Escherichia coliQ33966426
Dynamic interaction of the sec translocon with the chaperone PpiDQ33985391
Catabolic repression of secB expression is positively controlled by cyclic AMP (cAMP) receptor protein-cAMP complexes at the transcriptional levelQ33991514
A signal sequence is not required for protein export in prlA mutants of Escherichia coliQ34044995
PrlA suppressor mutations cluster in regions corresponding to three distinct topological domainsQ34058568
A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli.Q34058655
The ribosomal exit tunnel functions as a discriminating gateQ34118341
Degradation of a signal peptide by protease IV and oligopeptidase A.Q34164260
Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulationQ34309801
Physiological role during export for the retardation of folding by the leader peptide of maltose-binding proteinQ34322460
SecB is a bona fide generalized chaperone in Escherichia coliQ34336036
FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunitQ34342148
Localization of Polyribosomes Containing Alkaline Phosphatase Nascent Polypeptides on Membranes of Escherichia coliQ36768647
Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C terminiQ36769544
Protein secretion and membrane insertion systems in gram-negative bacteriaQ36839222
prl mutations in the Escherichia coli secG geneQ36844982
Crystal structure of a substrate-engaged SecY protein-translocation channelQ36865827
Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations.Q36910150
Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocationQ36932458
Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy TransferQ36942421
Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transferQ37029669
Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor speciesQ37031742
Translocon “Pulling” of Nascent SecM Controls the Duration of Its Translational Pause and Secretion-Responsive secA RegulationQ37051988
Energy transduction in protein transport and the ATP hydrolytic cycle of SecAQ37122860
The lateral gate of SecYEG opens during protein translocationQ37257359
Bacterial Sec protein transport is rate-limited by precursor length: a single turnover studyQ37369897
Mapping polypeptide interactions of the SecA ATPase during translocationQ37428012
Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocaseQ37445539
ATP is essential for protein translocation into Escherichia coli membrane vesiclesQ37522633
Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coliQ37557649
prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursorsQ37564839
In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coliQ37578783
Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane proteinQ37595620
SecD and SecF facilitate protein export in Escherichia coli.Q37628246
Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.Q37687646
The signal peptideQ37942677
Biophysical studies of signal peptides: implications for signal sequence functions and the involvement of lipid in protein exportQ37949458
The twin-arginine translocation (Tat) protein export pathwayQ38017546
The Type 1 secretion pathway - the hemolysin system and beyondQ38152930
Type V secretion: from biogenesis to biotechnologyQ38165623
Mechanism and structure of the bacterial type IV secretion systemsQ38175753
Type II secretion system: a magic beanstalk or a protein escalatorQ38175754
The membrane insertase YidC.Q38177989
Co-translational protein targeting to the bacterial membraneQ38186912
SecA-mediated targeting and translocation of secretory proteins.Q38192370
Synthesis and Transfer of Amylase in Pigeon Pancreatic MicrosomesQ72838986
The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzymeQ72932795
Maturation of exported proteins in Escherichia coli. Requirement for energy, site and kinetics of processingQ72939872
Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.Q54663164
Identification of potential active-site residues in the Escherichia coli leader peptidaseQ54676180
DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coliQ54676319
Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE proteinQ54682002
Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli.Q54695475
Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membranes.Q54696892
New suppressors of signal-sequence mutations, prlG, are linked tightly to the secE gene of Escherichia coli.Q54727879
Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.Q54738841
Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein.Q54740268
A functional decaisoleucine-containing signal sequence. Construction by cassette mutagenesis.Q54748298
Coupling between the sodium and proton gradients in respiring Escherichia coli cells measured by 23Na and 31P nuclear magnetic resonance.Q54779208
Atomic Model of the E.coli Membrane-bound Protein Translocation Complex SecYEGQ57840346
Disorder-order folding transitions underlie catalysis in the helicase motor of SecAQ57976550
A molecular switch in SecA protein couples ATP hydrolysis to protein translocationQ57976571
Separable ATPase and Membrane Insertion Domains of the SecA Subunit of Preprotein TranslocaseQ57976575
Non-bilayer Lipids Stimulate the Activity of the Reconstituted Bacterial Protein TranslocaseQ63359870
Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecAQ63359903
Interaction of SecB with soluble SecA 1Q63359914
Anionic phospholipids are essential for alpha-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesiclesQ67486006
Determination of a region in SecA that interacts with presecretory proteins in Escherichia coliQ67898246
Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfoldingQ67901010
A peptide corresponding to an export-defective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranesQ67926674
Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo functionQ68030460
Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivoQ68072417
The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coliQ68079685
Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative StructureQ68208733
In vitro protein translocation into inverted membrane vesicles prepared from Vibrio alginolyticus is stimulated by the electrochemical potential of Na+ in the presence of Escherichia coli SecAQ68459374
No specific recognition of leader peptide by SecB, a chaperone involved in protein exportQ68512094
SecE-dependent overproduction of SecY in Escherichia coli. Evidence for interaction between two components of the secretory machineryQ68534743
SecB protein stabilizes a translocation-competent state of purified prePhoE proteinQ69360855
SecA protein is directly involved in protein secretion in Escherichia coliQ69484198
Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation systemQ69484332
Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical propertiesQ69542568
In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factorQ70137148
Energy is required for maturation of exported proteins in Escherichia coliQ70159788
In vitro translocation of protein across Escherichia coli membrane vesicles requires both the proton motive force and ATPQ70166275
The biosynthesis of membrane-bound M13 coat protein. Energetics and assembly intermediatesQ70232037
A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteinsQ70244970
Energetics and intermediates of the assembly of Protein OmpA into the outer membrane of Escherichia coliQ70246320
Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongationQ70373251
Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocationQ71056385
Polysomes Extracted from Escherichia coli by Freeze-Thaw-Lysozyme LysisQ71189776
Regulation of a membrane component required for protein secretion in Escherichia coliQ71444140
Purification and characterization of leader (signal) peptidase from Escherichia coliQ72144849
Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12)Q72196641
Identification of the secY (prlA) gene product involved in protein export in Escherichia coliQ72409380
Genetic characterization of a gene for prolipoprotein signal peptidase in Escherichia coliQ72800486
P433issue2
P921main subjectEscherichia coliQ25419
P577publication date2017-11-01
P1433published inEcoSal PlusQ27725548
P1476titleThe Sec System: Protein Export in Escherichia coli
P478volume7

Reverse relations

cites work (P2860)
Q91892843Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion
Q57056828Co-assembly of SecYEG and SecA fully restores the properties of the native translocon
Q64898340Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers.
Q92510993Enhancing Recombinant Protein Yields in the E. coli Periplasm by Combining Signal Peptide and Production Rate Screening
Q89737499Escherichia coli Can Adapt Its Protein Translocation Machinery for Enhanced Periplasmic Recombinant Protein Production
Q91704513Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region
Q92867260Inner Membrane Translocases and Insertases
Q92601530Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome
Q58569559Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis
Q57463329Substrate Proteins Take Shape at an Improved Bacterial Translocon
Q64887171The Two Distinct Types of SecA2-Dependent Export Systems.

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