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Journal of Bacteriology, January 2009, p. 196-202, Vol. 191, No. 1
0021-9193/09/$08.00+0 doi:10.1128/JB.01264-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

and
Oscar P. Kuipers*
Molecular Genetics Group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands
Received 9 September 2008/ Accepted 23 October 2008
Protein translocation via the twin arginine translocation (TAT) pathway is characterized by the translocation of prefolded proteins across the hydrophobic lipid bilayer of the membrane. In Bacillus subtilis, two different Tat translocases are involved in this process, and both display different substrate specificities: PhoD is secreted via TatAdCd, whereas YwbN is secreted via TatAyCy. It was previously assumed that both TatAy and TatCy are essential for the translocation of the YwbN precursor. Through complementation studies, we now show that TatAy can be functionally replaced by TatAd when the latter is offered to the cells in excess amounts. Moreover, under conditions of overproduction, TatAdCd, in contrast to TatAyCy, shows an increased tolerance toward the acceptance of various Tat-dependent proteins.
Published ahead of print on 31 October 2008.
Present address: Department of Genetics, University Medical Center of Groningen, Groningen, The Netherlands.
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