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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.

SUBMITTER: van Wely KH

PROVIDER: S-EPMC93576 | biostudies-literature | 1999 Mar

REPOSITORIES: biostudies-literature

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

van Wely K H KH Swaving J J Broekhuizen C P CP Rose M M Quax W J WJ Driessen A J AJ

Journal of bacteriology 19990301 6

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 sensiti ...[more]

PMID: 10074070

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