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J. Biol. Chem., Vol. 278, Issue 18, 15622-15632, May 2, 2003
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,
From the Department of Genetics, Groningen Biomolecular Sciences
and Biotechnology Institute, P. O. Box 14, 9750 AA Haren, The
Netherlands and the In mitochondria, chloroplasts, and Gram-negative
eubacteria, Oxa1p(-like) proteins are critical for the biogenesis of
membrane proteins. Here we show that the Gram-positive eubacterium
Bacillus subtilis contains two functional Oxa1p
orthologues, denoted SpoIIIJ and YqjG. The presence of either SpoIIIJ
or YqjG is required for cell viability. Whereas SpoIIIJ is required for
sporulation, YqjG is dispensable for this developmental process. The
stability of two membrane proteins was found to be mildly affected upon
SpoIIIJ limitation in the absence of YqjG. Surprisingly, the topology and stability of other membrane proteins remained unaffected under these conditions. In contrast, SpoIIIJ- and YqjG-limiting conditions resulted in a strong post-translocational defect in the stability of
secretory proteins. Together, these data indicate that SpoIIIJ and YqjG
of B. subtilis are involved in both membrane
protein biogenesis and protein secretion. However, the reduced
stability of secretory proteins seems to be the most prominent
phenotype of SpoIIIJ/YqjG-depleted B. subtilis cells.
In conclusion, our observations show that SpoIIIJ and YqjG have
different, but overlapping functions in B. subtilis. Most importantly, it seems that different members of the Oxa1p protein family have acquired at least partly distinct, species-specific, functions that are essential for life.
Department of Pharmaceutical Biology,
University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands
Supported by Genencor International (Leiden, The Netherlands).
§
Supported in part by European Union Grants QLK3-CT-1999-00413 and
QLK3-CT-1999-00917.
¶
To whom correspondence should be addressed. Tel.: 31503632105;
Fax: 31503632348; E-mail: S.Bron@biol.rug.nl.
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