Localization of SpoVAD to the Inner Membrane of Spores of Bacillus Subtilis

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 2005 Aug 4

PMID 16077113

Citations 38

Authors

Venkata Ramana Vepachedu

Peter Setlow

Affiliations

Soon will be listed here.

Abstract

The products of the hexacistronic spoVA operon of Bacillus subtilis may be involved in the transport of dipicolinic acid into the forespore during sporulation and its release during spore germination. The major hydrophilic coding region of B. subtilis spoVAD was cloned, the protein was expressed in Escherichia coli as a His tag fusion protein, and a rabbit antiserum was raised against the purified protein. Western blot analyses of fractions from B. subtilis spores showed that SpoVAD is an integral inner membrane protein present at levels >50-fold higher than those of the spore's nutrient germinant receptors that are also present in the inner membrane. SpoVAD also persisted in outgrowing spores.

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