The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. (Q41006640)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9321390%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

title

The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation (English)

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6 November 2019

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6 November 2019

P Fekkes

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6 November 2019

C van der Does

series ordinal

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6 November 2019

language of work or name

English

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publication date

1 October 1997

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6 November 2019

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6 November 2019

volume

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6 November 2019

issue

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6 November 2019

page(s)

6105-6113

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Protein measurement with the Folin phenol reagent

6 November 2019

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins

26 September 2017

1 reference

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Electrospray mass spectrometric investigation of the chaperone SecB.

26 September 2017

1 reference

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Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo

26 September 2017

1 reference

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Translocation can drive the unfolding of a preprotein domain.

26 September 2017

1 reference

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Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature.

26 September 2017

1 reference

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How proteins cross the bacterial cytoplasmic membrane.

26 September 2017

1 reference

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SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase

26 September 2017

1 reference

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Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB.

26 September 2017

1 reference

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Whole-genome random sequencing and assembly of Haemophilus influenzae Rd

26 September 2017

1 reference

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E. coli mutant pleiotropically defective in the export of secreted proteins

26 September 2017

1 reference

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Studies on transformation of Escherichia coli with plasmids

26 September 2017

1 reference

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT.

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

The enzymology of protein translocation across the Escherichia coli plasma membrane

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Molecular chaperones and protein translocation across the Escherichia coli inner membrane

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Bacterial protein translocation: kinetic and thermodynamic role of ATP and the protonmotive force

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: endoproteolytic cleavage of nascent f1 pre-coat protein

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm.

26 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Identification of a soluble SecA/SecB complex by means of a subfractionated cell-free export system.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the protonmotive force.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Domain interactions of the peripheral preprotein Translocase subunit SecA.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

The C terminus of SecA is involved in both lipid binding and SecB binding.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Sequence analysis of a DNA fragment from Buchnera aphidicola (an endosymbiont of aphids) containing genes homologous to dnaG, rpoD, cysE, and secB

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1326294

Characterization of Escherichia coli SecA protein binding to a site on its mRNA involved in autoregulation

19 August 2018

1 reference

12 December 2020

Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative Structure

1 reference

12 December 2020

Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo

1 reference

12 December 2020

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

12 December 2020

Separable ATPase and Membrane Insertion Domains of the SecA Subunit of Preprotein Translocase

1 reference

12 December 2020

Identifiers

DOI

10.1093/EMBOJ/16.20.6105

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9321390%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9321390%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

PubMed publication ID

9321390

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9321390%20AND%20SRC:MED&resulttype=core&format=json