The structural view of bacterial translocation-specific chaperone SecB: implications for function (Q34455348)

2 August 2017

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title

The structural view of bacterial translocation-specific chaperone SecB: implications for function (English)

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2 August 2017

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Jiahai Zhou

1

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2 August 2017

Zhaohui Xu

series ordinal

2

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2 August 2017

language of work or name

English

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publication date

1 October 2005

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2 August 2017

published in

Molecular Microbiology

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2 August 2017

volume

58

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2 August 2017

issue

2

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2 August 2017

page(s)

349-357

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Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.

2 August 2017

cites work

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

In-vitro studies on the folding characteristics of the Escherichia coli precursor protein prePhoE. Evidence that SecB prevents the precursor from aggregating by forming a functional complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

SecB-binding does not maintain the translocation-competent state of prePhoE

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Crystal structure of SecB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Solution NMR structure and X-ray absorption analysis of the C-terminal zinc-binding domain of the SecA ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

SecB, a molecular chaperone with two faces

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

The structural basis of protein targeting and translocation in bacteria.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Zinc stabilizes the SecB binding site of SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Functional identification of the SecB homologue in Methanococcus jannaschii and direct interaction of SecB with trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Dimeric SecA is essential for protein translocation

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Mapping of the Binding Frame for the Chaperone SecB within a Natural Ligand, Galactose-binding Protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Sec-dependent protein export and the involvement of the molecular chaperone SecB.

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Substrate specificity of the SecB chaperone

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Escherichia coli SecB protein associates with exported protein precursors in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

NMR structure of the C-terminal domain of SecA in the free state.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

The bacterial ATPase SecA functions as a monomer in protein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

A large conformational change of the translocation ATPase SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

High selectivity with low specificity: how SecB has solved the paradox of chaperone binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

SecB, one small chaperone in the complex milieu of the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Sites of interaction between SecA and the chaperone SecB, two proteins involved in export

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporter

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Determination of the binding frame within a physiological ligand for the chaperone SecB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

SecB is a bona fide generalized chaperone in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Crystal structure of the bacterial protein export chaperone secB

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

Structural determinants of SecB recognition by SecA in bacterial protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1365-2958.2005.04842.X

10.1111/J.1365-2958.2005.04842.X

21 January 2018

Identifiers

DOI

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2 August 2017

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