SecB-A chaperone dedicated to protein translocation

Philipp Bechtluft; Nico Nouwen; Sander J. Tans; Arnold J.M. Driessen

doi:10.1039/B915435C

SecB-A chaperone dedicated to protein translocation

Philipp Bechtluft, Nico Nouwen, Sander J. Tans, Arnold J.M. Driessen

Research output: Contribution to journal › Review article › peer-review

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Abstract

SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.

Original language	English
Pages (from-to)	620-627
Number of pages	8
Journal	Molecular BioSystems
Volume	6
Issue number	4
DOIs	https://doi.org/10.1039/B915435C
Publication status	Published - 2010

Keywords

MALTOSE-BINDING PROTEIN
BACTERIAL CYTOPLASMIC MEMBRANE
ESCHERICHIA-COLI
SIGNAL SEQUENCE
ANTIFOLDING ACTIVITY
DENATURED PROTEINS
SUBSTRATE PROTEIN
CRYSTAL-STRUCTURE
FOLDING PATHWAY
TRIGGER FACTOR

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SecB—A chaperone dedicated to protein translocation
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@article{3b321cb30267495abc06998ea09f53ab,

title = "SecB-A chaperone dedicated to protein translocation",

abstract = "SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.",

keywords = "MALTOSE-BINDING PROTEIN, BACTERIAL CYTOPLASMIC MEMBRANE, ESCHERICHIA-COLI, SIGNAL SEQUENCE, ANTIFOLDING ACTIVITY, DENATURED PROTEINS, SUBSTRATE PROTEIN, CRYSTAL-STRUCTURE, FOLDING PATHWAY, TRIGGER FACTOR",

author = "Philipp Bechtluft and Nico Nouwen and Tans, {Sander J.} and Driessen, {Arnold J.M.}",

note = "Relation: http://www.rug.nl/gbb/ Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute",

year = "2010",

doi = "10.1039/B915435C",

language = "English",

volume = "6",

pages = "620--627",

journal = "Molecular BioSystems",

issn = "1742-206X",

publisher = "ROYAL SOC CHEMISTRY",

number = "4",

}

TY - JOUR

T1 - SecB-A chaperone dedicated to protein translocation

AU - Bechtluft, Philipp

AU - Nouwen, Nico

AU - Tans, Sander J.

AU - Driessen, Arnold J.M.

N1 - Relation: http://www.rug.nl/gbb/ Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute

PY - 2010

Y1 - 2010

N2 - SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.

AB - SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.

KW - MALTOSE-BINDING PROTEIN

KW - BACTERIAL CYTOPLASMIC MEMBRANE

KW - ESCHERICHIA-COLI

KW - SIGNAL SEQUENCE

KW - ANTIFOLDING ACTIVITY

KW - DENATURED PROTEINS

KW - SUBSTRATE PROTEIN

KW - CRYSTAL-STRUCTURE

KW - FOLDING PATHWAY

KW - TRIGGER FACTOR

U2 - 10.1039/B915435C

DO - 10.1039/B915435C

M3 - Review article

SN - 1742-206X

VL - 6

SP - 620

EP - 627

JO - Molecular BioSystems

JF - Molecular BioSystems

IS - 4

ER -