Functional identification of the product of the Bacillus subtilis yvaL gene as a SecG homologue.

Abstract:

:Protein export in Escherichia coli is mediated by translocase, a multisubunit membrane protein complex with SecA as the peripheral subunit and the SecY, SecE, and SecG proteins as the integral membrane domain. In the gram-positive bacterium Bacillus subtilis, SecA, SecY, and SecE have been identified through genetic analysis. Sequence comparison of the Bacillus chromosome identified a potential homologue of SecG, termed YvaL. A chromosomal disruption of the yvaL gene results in mild cold sensitivity and causes a beta-lactamase secretion defect. The cold sensitivity is exacerbated by overexpression of the secretory protein alpha-amylase, whereas growth and beta-lactamase secretion are restored by coexpression of yvaL or the E. coli secG gene. These results indicate that the yvaL gene codes for a protein that is functionally homologous to SecG.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

van Wely KH,Swaving J,Broekhuizen CP,Rose M,Quax WJ,Driessen AJ

doi

10.1128/JB.181.6.1786-1792.1999

keywords:

subject

Has Abstract

pub_date

1999-03-01 00:00:00

pages

1786-92

issue

6

eissn

0021-9193

issn

1098-5530

journal_volume

181

pub_type

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