JB Accepts, published online ahead of print on 2 November 2007

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J. Bacteriol. doi:10.1128/JB.01482-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Determinants for the Subcellular Localization and Function of a Non-essential SEDS protein

Gonçalo Real, Allison Fay, Avigdor Eldar, Sérgio M. Pinto, Adriano O. Henriques, and Jonathan Dworkin^*

Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, Apartado 127, 2781-901 Oeiras, PORTUGAL; Department of Microbiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032; Division of Biology, California Institute of Technology, Pasadena, CA 94703

^* To whom correspondence should be addressed. Email: jonathan.dworkin{at}columbia.edu.

The B. subtilis SpoVE integral membrane protein is essential for the heat resistance of spores probably because of its involvement in spore peptidoglycan synthesis. We found that a SpoVE-YFP fusion protein becomes localized to the forespore during the earliest stages of engulfment, and this pattern is maintained throughout sporulation. SpoVE belongs to a well-conserved family of proteins that includes the FtsW and RodA proteins of B. subtilis. These proteins are involved in bacterial shape determination, although their function is not known. FtsW is necessary for the formation of the asymmetric septum in sporulation, and we found that an FtsW-YFP fusion localized to this structure, prior to the initiation of engulfment in a non-overlapping pattern with SpoVE-CFP. Since FtsW and RodA are essential for normal growth, it has not been possible to identify loss-of-function mutations that would greatly facilitate analysis of their function. We took advantage of the fact that SpoVE is not required for growth to obtain point mutations in SpoVE that block the development of spore heat resistance, but that allow normal protein expression and targeting to the forespore. These mutant proteins will be invaluable tools for future experiments aimed at elucidating the function of members of the SEDS family of proteins.

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