SecB--a chaperone dedicated to protein translocation. (Q37710987)

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20 January 2020

review article

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title

SecB--a chaperone dedicated to protein translocation (English)

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20 January 2020

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20 January 2020

2

Nico Nouwen

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20 January 2020

3

Sander J Tans

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20 January 2020

author name string

Philipp Bechtluft

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1

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20 January 2020

publication date

19 October 2009

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20 January 2020

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volume

6

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issue

4

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20 January 2020

page(s)

620-627

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Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA

20 January 2020

cites work

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The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein

21 January 2018

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

21 January 2018

1 reference

The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro

21 January 2018

1 reference

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

21 January 2018

1 reference

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

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

21 January 2018

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Zinc stabilizes the SecB binding site of SecA.

21 January 2018

1 reference

Crystal structure of the bacterial protein export chaperone secB

21 January 2018

1 reference

Structural determinants of SecB recognition by SecA in bacterial protein translocation

21 January 2018

1 reference

Defining the role of the Escherichia coli chaperone SecB using comparative proteomics.

21 January 2018

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Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling

21 January 2018

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Direct observation of chaperone-induced changes in a protein folding pathway

21 January 2018

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Crystal structure of SecB from Escherichia coli

21 January 2018

1 reference

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

21 January 2018

1 reference

The twin-arginine transport system: moving folded proteins across membranes

21 January 2018

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Protein translocation across the bacterial cytoplasmic membrane.

21 January 2018

1 reference

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

Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins

21 January 2018

1 reference

SecB is a bona fide generalized chaperone in Escherichia coli

21 January 2018

1 reference

Translocation of proteins across the cell envelope of Gram-positive bacteria

21 January 2018

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

21 January 2018

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Substrate specificity of the SecB chaperone

21 January 2018

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Calorimetric analyses of the interaction between SecB and its ligands

21 January 2018

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

21 January 2018

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Kinetics and energetics of the translocation of maltose binding protein folding mutants

21 January 2018

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SecB-mediated protein export need not occur via kinetic partitioning

21 January 2018

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Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

21 January 2018

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Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

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

21 January 2018

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Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA

21 January 2018

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

21 January 2018

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prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli

21 January 2018

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Two cellular components, PrlA and SecB, that recognize different sequence determinants are required for efficient protein export

21 January 2018

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Escherichia coli SecB stimulates export without maintaining export competence of ribose-binding protein signal sequence mutants.

21 January 2018

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Influence of impaired chaperone or secretion function on SecB production in Escherichia coli

21 January 2018

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

21 January 2018

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Folded HasA inhibits its own secretion through its ABC exporter

21 January 2018

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

21 January 2018

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