The bacterial Sec-translocase: structure and mechanism

Jelger A. Lycklama a Nijeholt; Arnold J. M. Driessen

doi:10.1098/rstb.2011.0201

The bacterial Sec-translocase: structure and mechanism

Jelger A. Lycklama a Nijeholt, Arnold J. M. Driessen^*

^*Corresponding author for this work

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

116 Citations (Scopus)

18 Downloads (Pure)

Abstract

Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP-dependent motor protein SecA. The ancillary SecDF membrane protein complex promotes the final stages of translocation. Recent years have seen a major advance in our understanding of the structural and biochemical basis of protein translocation, and this has led to a detailed model of the translocation mechanism.

Original language	English
Pages (from-to)	1016-1028
Number of pages	13
Journal	Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
Volume	367
Issue number	1592
DOIs	https://doi.org/10.1098/rstb.2011.0201
Publication status	Published - 19-Apr-2012

Keywords

protein translocation
membrane protein insertion
SecY
translocon
SecA
SIGNAL-SEQUENCE RECOGNITION
PRECURSOR PROTEIN TRANSLOCATION
ESCHERICHIA-COLI TRANSLOCASE
LARGE CONFORMATIONAL-CHANGE
BACILLUS-SUBTILIS SECA
ATP-BINDING-SITE
X-RAY-STRUCTURE
PLUG DOMAIN
PREPROTEIN TRANSLOCASE
ENDOPLASMIC-RETICULUM

Access to Document

10.1098/rstb.2011.0201

Handle.net

Persistent link

Embargoed Document

The bacterial Sec-translocase structure and mechanism
Final publisher's version, 906 KB
Request copy

Cite this

@article{2fffac73b99e476ba10f83309b9f4898,

title = "The bacterial Sec-translocase: structure and mechanism",

abstract = "Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP-dependent motor protein SecA. The ancillary SecDF membrane protein complex promotes the final stages of translocation. Recent years have seen a major advance in our understanding of the structural and biochemical basis of protein translocation, and this has led to a detailed model of the translocation mechanism.",

keywords = "protein translocation, membrane protein insertion, SecY, translocon, SecA, SIGNAL-SEQUENCE RECOGNITION, PRECURSOR PROTEIN TRANSLOCATION, ESCHERICHIA-COLI TRANSLOCASE, LARGE CONFORMATIONAL-CHANGE, BACILLUS-SUBTILIS SECA, ATP-BINDING-SITE, X-RAY-STRUCTURE, PLUG DOMAIN, PREPROTEIN TRANSLOCASE, ENDOPLASMIC-RETICULUM",

author = "{Lycklama a Nijeholt}, {Jelger A.} and Driessen, {Arnold J. M.}",

year = "2012",

month = apr,

day = "19",

doi = "10.1098/rstb.2011.0201",

language = "English",

volume = "367",

pages = "1016--1028",

journal = "Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences",

issn = "0962-8436",

publisher = "ROYAL SOC",

number = "1592",

}

TY - JOUR

T1 - The bacterial Sec-translocase

T2 - structure and mechanism

AU - Lycklama a Nijeholt, Jelger A.

AU - Driessen, Arnold J. M.

PY - 2012/4/19

Y1 - 2012/4/19

N2 - Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP-dependent motor protein SecA. The ancillary SecDF membrane protein complex promotes the final stages of translocation. Recent years have seen a major advance in our understanding of the structural and biochemical basis of protein translocation, and this has led to a detailed model of the translocation mechanism.

AB - Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP-dependent motor protein SecA. The ancillary SecDF membrane protein complex promotes the final stages of translocation. Recent years have seen a major advance in our understanding of the structural and biochemical basis of protein translocation, and this has led to a detailed model of the translocation mechanism.

KW - protein translocation

KW - membrane protein insertion

KW - SecY

KW - translocon

KW - SecA

KW - SIGNAL-SEQUENCE RECOGNITION

KW - PRECURSOR PROTEIN TRANSLOCATION

KW - ESCHERICHIA-COLI TRANSLOCASE

KW - LARGE CONFORMATIONAL-CHANGE

KW - BACILLUS-SUBTILIS SECA

KW - ATP-BINDING-SITE

KW - X-RAY-STRUCTURE

KW - PLUG DOMAIN

KW - PREPROTEIN TRANSLOCASE

KW - ENDOPLASMIC-RETICULUM

U2 - 10.1098/rstb.2011.0201

DO - 10.1098/rstb.2011.0201

M3 - Review article

SN - 0962-8436

VL - 367

SP - 1016

EP - 1028

JO - Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences

JF - Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences

IS - 1592

ER -