SecA dimer cross-linked at its subunit interface is functional for protein translocation.

Abstract:

:SecA facilitates protein transport across the eubacterial plasma membrane by its association with cargo proteins and the SecYEG translocon, followed by ATP-driven conformational changes that promote protein translocation in a stepwise manner. Whether SecA functions as a monomer or a dimer during this process has been the subject of considerable controversy. Here we utilize cysteine-directed mutagenesis along with the crystal structure of the SecA dimer to create a cross-linked dimer at its subunit interface, which was normally active for in vitro protein translocation.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Jilaveanu LB,Oliver D

doi

10.1128/JB.188.1.335-338.2006

keywords:

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

335-8

issue

1

eissn

0021-9193

issn

1098-5530

pii

188/1/335

journal_volume

188

pub_type

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