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Journal of Bacteriology, November 2009, p. 6749-6757, Vol. 191, No. 21
0021-9193/09/$08.00+0     doi:10.1128/JB.00853-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Bacillus subtilis SpoIIIJ and YqjG Function in Membrane Protein Biogenesis{triangledown}

Manfred J. Saller,1 Fabrizia Fusetti,2 and Arnold J. M. Driessen1*

Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, Kluyver Centre for the Genomics of Industrial Fermentations and the Zernike Institute of Advanced Materials, University of Groningen, 9751 NN Haren, The Netherlands,1 Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands2

Received 29 June 2009/ Accepted 17 August 2009

In all domains of life Oxa1p-like proteins are involved in membrane protein biogenesis. Bacillus subtilis, a model organism for gram-positive bacteria, contains two Oxa1p homologs: SpoIIIJ and YqjG. These molecules appear to be mutually exchangeable, although SpoIIIJ is specifically required for spore formation. SpoIIIJ and YqjG have been implicated in a posttranslocational stage of protein secretion. Here we show that the expression of either spoIIIJ or yqjG functionally compensates for the defects in membrane insertion due to YidC depletion in Escherichia coli. Both SpoIIIJ and YqjG complement the function of YidC in SecYEG-dependent and -independent membrane insertion of subunits of the cytochrome o oxidase and F1Fo ATP synthase complexes. Furthermore, SpoIIIJ and YqjG facilitate membrane insertion of F1Fo ATP synthase subunit c from both E. coli and B. subtilis into inner membrane vesicles of E. coli. When isolated from B. subtilis cells, SpoIIIJ and YqjG were found to be associated with the entire F1Fo ATP synthase complex, suggesting that they have a role late in the membrane assembly process. These data demonstrate that the Bacillus Oxa1p homologs have a role in membrane protein biogenesis rather than in protein secretion.

* Corresponding author. Mailing address: Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, Kluyver Centre for the Genomics of Industrial Fermentations and the Zernike Institute of Advanced Materials, University of Groningen, 9751 NN Haren, The Netherlands. Phone and fax: 31-50-3632164. E-mail: a.j.m.driessen{at}rug.nl

{triangledown} Published ahead of print on 28 August 2009.

Journal of Bacteriology, November 2009, p. 6749-6757, Vol. 191, No. 21
0021-9193/09/$08.00+0     doi:10.1128/JB.00853-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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