Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain

scientific article published on 30 November 2012

Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/JB.02032-12
P932PMC publication ID3562099
P698PubMed publication ID23204463

P2093author name stringMiriam Braunstein
Henry S Gibbons
Lauren S Ligon
Meghan E Feltcher
P2860cites workOverlapping functions of components of a bacterial Sec-independent protein export pathwayQ24533263
SecA, a remarkable nanomachineQ24631210
Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMRQ27649095
A common export pathway for proteins binding complex redox cofactors?Q27976517
Signal peptidasesQ28217085
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
SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosisQ28487244
ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophagesQ28487421
Mycobacterium tuberculosis Rv2224c modulates innate immune responsesQ28487461
SignalP 4.0: discriminating signal peptides from transmembrane regionsQ29547202
Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatisQ29615255
SecA-dependent quality control of intracellular protein localizationQ31022756
Investigating the role of secA2 in secretion and glycosylation of a fimbrial adhesin in Streptococcus parasanguis FW213.Q31095089
Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathwayQ33232877
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coliQ33562047
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
Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transferQ33773458
Competition between Sec- and TAT-dependent protein translocation in Escherichia coliQ33890978
Translocation can drive the unfolding of a preprotein domain.Q34041521
Transport of preproteins by the accessory Sec system requires a specific domain adjacent to the signal peptideQ34045689
Modeling the effects of prl mutations on the Escherichia coli SecY complexQ34048338
The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamasesQ34124354
SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosisQ35003009
Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathwayQ35022917
The antigen 85 complex: a major secretion product of Mycobacterium tuberculosisQ35655414
Selective photoaffinity labeling identifies the signal peptide binding domain on SecAQ35750297
The bacterial Sec-translocase: structure and mechanism.Q35814696
Glycine residues in the hydrophobic core of the GspB signal sequence route export toward the accessory Sec pathwayQ35879231
A little help from my friends: quality control of presecretory proteins in bacteriaQ35933897
A genomic view of sugar transport in Mycobacterium smegmatis and Mycobacterium tuberculosisQ35949975
A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec systemQ36097994
Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysis of a mycobacterial lgt mutant.Q36156186
Emerging themes in SecA2-mediated protein exportQ36206572
Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasmQ36313695
Mutations in a new gene, secB, cause defective protein localization in Escherichia coliQ36326983
SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesisQ36350571
Evidence for specificity at an early step in protein export in Escherichia coliQ36361933
The bacterial twin-arginine translocation pathwayQ36498300
Prediction of lipoprotein signal peptides in Gram-negative bacteriaQ36572165
Characterization of the accessory Sec system of Staphylococcus aureusQ36898397
Beta-lactamase can function as a reporter of bacterial protein export during Mycobacterium tuberculosis infection of host cellsQ37082058
Molecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulenceQ37232681
Mapping polypeptide interactions of the SecA ATPase during translocationQ37428012
SecA: a tale of two protomersQ37742750
The signal peptideQ37942677
The twin-arginine translocation (Tat) protein export pathwayQ38017546
Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coliQ38290685
The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation eventsQ38339927
The antifolding activity of SecB promotes the export of the E. coli maltose-binding proteinQ38347439
Two nonredundant SecA homologues function in mycobacteria.Q39505468
Genetic Analysis of Pathway Specificity during Posttranslational Protein Translocation across the Escherichia coli Plasma MembraneQ39750256
Identification of a regulated alkaline phosphatase, a cell surface-associated lipoprotein, in Mycobacterium smegmatis.Q39793904
SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial proteinQ40388434
The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipidsQ40871781
Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathwayQ42412477
Identification of the preprotein binding domain of SecA.Q42485674
The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane sealQ42621979
Differential roles of individual domains in selection of secretion route of a Streptococcus parasanguinis serine-rich adhesin, Fap1.Q42910236
The Accessory SecA2 System of Mycobacteria Requires ATP Binding and the Canonical SecA1.Q43150590
A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motifQ43858288
Genetic analysis of the beta-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to beta-lactam antibioticsQ45256213
An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets.Q45947385
Determinants of the streptococcal surface glycoprotein GspB that facilitate export by the accessory Sec system.Q45992753
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.Q46008320
Targeting of unfolded PhoA to the TAT translocon of Escherichia coliQ46786492
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.Q52513940
The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism.Q53410084
Bacterial sec-translocase unfolds and translocates a class of folded protein domains.Q54437009
The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coliQ57839654
Determination of a region in SecA that interacts with presecretory proteins in Escherichia coliQ67898246
Lipoprotein antigens of Mycobacterium tuberculosisQ67992293
Genetic methods for deciphering virulence determinants of Mycobacterium tuberculosisQ78635273
P433issue4
P407language of work or nameEnglishQ1860
P1104number of pages10
P304page(s)672-681
P577publication date2012-11-30
P1433published inJournal of BacteriologyQ478419
P1476titleProtein export by the mycobacterial SecA2 system is determined by the preprotein mature domain
P478volume195

Reverse relations

cites work (P2860)
Q35074917A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants
Q37267515An orphaned Mce-associated membrane protein of Mycobacterium tuberculosis is a virulence factor that stabilizes Mce transporters.
Q54403588Analysis of SecA2-dependent substrates in Mycobacterium marinum identifies protein kinase G (PknG) as a virulence effector.
Q36028567Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly
Q36245018Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface
Q40422734Divergent Functions of TLR2 on Hematopoietic and Nonhematopoietic Cells during Chronic Mycobacterium tuberculosis Infection
Q36650627Genetic features of Mycobacterium tuberculosis modern Beijing sublineage
Q27680634Genetic regulation of vesiculogenesis and immunomodulation in Mycobacterium tuberculosis
Q92350578Hot and Cold Spot Areas of Household Tuberculosis Transmission in Southern China: Effects of Socio-Economic Status and Mycobacterium tuberculosis Genotypes
Q35692102Label-free Quantitative Proteomics Reveals a Role for the Mycobacterium tuberculosis SecA2 Pathway in Exporting Solute Binding Proteins and Mce Transporters to the Cell Wall
Q38258834Mycobacterium tuberculosis evolutionary pathogenesis and its putative impact on drug development
Q60921483SatS is a chaperone for the SecA2 protein export pathway
Q38208070Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond
Q38159106Selective transport by SecA2: an expanding family of customized motor proteins
Q36575070Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.
Q37253035Suppressor analysis reveals a role for SecY in the SecA2-dependent protein export pathway of Mycobacteria
Q38827839The Canonical and Accessory Sec System of Gram-positive Bacteria.
Q35168922The Mycobacterium tuberculosis outer membrane channel protein CpnT confers susceptibility to toxic molecules
Q64887171The Two Distinct Types of SecA2-Dependent Export Systems.
Q48250974The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY.
Q34070493The non-catalytic "cap domain" of a mycobacterial metallophosphoesterase regulates its expression and localization in the cell
Q38639041Understanding HIV-Mycobacteria synergism through comparative proteomics of intra-phagosomal mycobacteria during mono- and HIV co-infection

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