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Journal of Bacteriology, March 1999, p. 1786-1792, Vol. 181, No. 6
Department of Microbiology,
Received 28 September 1998/Accepted 4 January 1999
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
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Functional Identification of the Product of the Bacillus
subtilis yvaL Gene as a SecG Homologue
-lactamase secretion defect. The cold
sensitivity is exacerbated by overexpression of the secretory protein
-amylase, whereas growth and
-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.
*
Corresponding author. Mailing address: Department of
Microbiology, Groningen Biomolecular Sciences and Biotechnology
Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The
Netherlands. Phone: 31 50 3632164. Fax: 31 50 3632154. E-mail:
a.j.m.driessen{at}biol.rug.nl.
Journal of Bacteriology, March 1999, p. 1786-1792, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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