Dynamic action of the Sec machinery during initiation, protein translocation and termination.

scientific article published on 7 June 2018

Dynamic action of the Sec machinery during initiation, protein translocation and termination. is …
instance of (P31):
scholarly articleQ13442814

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P5530Altmetric DOI10.7554/ELIFE.35112
P6179Dimensions Publication ID1104437803
P356DOI10.7554/ELIFE.35112
P953full work available at URLhttp://eprints.whiterose.ac.uk/131829/
P6366Microsoft Academic ID2805415035
P932PMC publication ID6021171
P698PubMed publication ID29877797
P1154Scopus EID2-s2.0-85051967446

P50authorSheena RadfordQ17011933
Daniel W WatkinsQ63360021
William J AllenQ80738070
Tomás FesslQ84379568
Ian CollinsonQ47451336
Peter OatleyQ56422836
Jim HorneQ56422837
Roman TumaQ63347451
Robin A CoreyQ41551886
P2093author name stringSteve A Baldwin
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Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound StateQ27702712
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A "push and slide" mechanism allows sequence-insensitive translocation of secretory proteins by the SecA ATPaseQ42209016
Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocationQ42576947
Synthetic peptides identify a second periplasmic site for the plug of the SecYEG protein translocation complexQ42606260
Conformations of signal peptides induced by lipids suggest initial steps in protein exportQ43627974
Kinetic analysis of the translocation of fluorescent precursor proteins into Escherichia coli membrane vesicles.Q44133891
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.Q46008320
The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membraneQ46059428
Sequence analysis of mutations that prevent export of lambda receptor, an Escherichia coli outer membrane protein.Q48413526
SecA supports a constant rate of preprotein translocation.Q54467339
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The oligomeric state and arrangement of the active bacterial transloconQ30498189
Shot-noise limited single-molecule FRET histograms: comparison between theory and experimentsQ30499969
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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
Quantifying heterogeneity and conformational dynamics from single molecule FRET of diffusing molecules: recurrence analysis of single particles (RASP).Q33789209
Overproduction of SecA suppresses the export defect caused by a mutation in the gene encoding the Escherichia coli export chaperone secB.Q33991984
Structure and function of the bacterial Sec translocon.Q34005867
Translocation can drive the unfolding of a preprotein domain.Q34041521
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Quantitative interpretation of FRET experiments via molecular simulation: force field and validationQ35688357
Monitoring conformational dynamics of a single molecule by selective fluorescence spectroscopy.Q35872871
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
Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complexQ36455887
Crystal structure of a substrate-engaged SecY protein-translocation channelQ36865827
Energy transduction in protein transport and the ATP hydrolytic cycle of SecAQ37122860
Bacterial Sec protein transport is rate-limited by precursor length: a single turnover studyQ37369897
Conformational and membrane-binding properties of a signal sequence are largely unaltered by its adjacent mature regionQ37541742
Domain movements of the enhancer-dependent sigma factor drive DNA delivery into the RNA polymerase active site: insights from single molecule studiesQ37734330
The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation eventsQ38339927
Different exported proteins in E. coli show differences in the temporal mode of processing in vivoQ38356214
Analysis of polypeptide movement in the SecY channel during SecA-mediated protein translocationQ38791583
Toward a structural understanding of co-translational protein translocationQ38828338
Investigating the SecY plug movement at the SecYEG translocation channel.Q39470287
Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linkingQ39495963
Skp is a multivalent chaperone of outer-membrane proteinsQ39562461
Unlocking the Bacterial SecY TransloconQ39923654
The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE.Q40805905
Structure of the SecY complex unlocked by a preprotein mimic.Q42000002
P4510describes a project that usesscikit-imageQ22442795
P407language of work or nameEnglishQ1860
P577publication date2018-06-07
P1433published ineLifeQ2000008
P859sponsorDeciphering the allosteric mechanism of protein translocation through membranesQ63368563
P1476titleDynamic action of the Sec machinery during initiation, protein translocation and termination
P478volume7

Reverse relations

cites work (P2860)
Q61451642ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery
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
Q90044373Dynamics of Co-translational Membrane Protein Integration and Translocation via the Sec Translocon
Q91555669Free-energy landscapes of membrane co-translocational protein unfolding
Q83231318HDX-MS reveals nucleotide-dependent, anti-correlated opening and closure of SecA and SecY channels of the bacterial translocon
Q94483980Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients
Q64106021Omnipresent Maxwell's demons orchestrate information management in living cells
Q92401978Protein translocation by the SecA ATPase occurs by a power-stroke mechanism
Q57463329Substrate Proteins Take Shape at an Improved Bacterial Translocon
Q91638430The Dynamic ATP-Driven Mechanism of Bacterial Protein Translocation and the Critical Role of Phospholipids
Q92703990Voltage Sensing in Bacterial Protein Translocation

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