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The carboxyl terminus of the Bacillus subtilis SecA is dispensable for protein secretion and viability

Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands¹
Institut für Biotechnologie 1, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany²

Author for correspondence: Arnold J. M. Driessen. Tel: +31 50 3632164. Fax: +31 50 3632154. e-mail: a.j.m.driessen{at}biol.rug.nl

The Escherichia coli secretion-dedicated chaperone SecB targets a subset of proteins to the translocase by interacting with the carboxyl (C-) terminus of SecA. This region of SecA is highly conserved in Eubacteria, but despite its presence in the Bacillus subtilis SecA, the B. subtilis genome does not appear to contain a gene for a clear homologue of SecB. Deletion of the C-terminus of the B. subtilis SecA yields cells that have normal viability, but that exhibit a response reminiscent of oxidative stress and the loss of a number of secretory proteins from the culture supernatant. Semi-quantitative RT-PCR demonstrates that these proteins are expressed at lower levels. The C-terminus of SecA fused to glutathione S-transferase (GST) specifically binds a cytosolic protein, termed MrgA. This protein has been reported to function in relation to oxidative stress, but deletion of the mrgA gene does not result in a secretion defect nor does it cause an oxidative stress response. It is concluded that the C-terminus of the B. subtilis SecA is not essential for secretion and viability.

Keywords: protein secretion, chaperones, SecA, SecB

Abbreviations: Cam, chloramphenicol; GST, Schistosoma japonicum glutathione S-transferase; GST-C, GST fusion bearing the C-terminal 22 amino acids of B. subtilis SecA; Phle, phleomycin; SRP, signal recognition particle

^a Present address: Department of Experimental Pathology, Josephine Nefkens Institute, Erasmus University Rotterdam, PO Box 1738, 3000 DR Rotterdam, The Netherlands.

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