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J Mol Biol. 2009 Mar 6;386(4):962-75. doi: 10.1016/j.jmb.2008.10.061. Epub 2008 Oct 30.

Crystal structure of SpoVT, the final modulator of gene expression during spore development in Bacillus subtilis.

Author information

1
Department of Membrane Biochemistry, Max Planck Institute for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.

Abstract

Endospore formation in Bacillus subtilis is orchestrated by five developmental sigma factors and further modulated by several auxiliary transcription factors. One of these, SpoVT, regulates forespore-specific sigma(G)-dependent genes and plays a key role in the final stages of spore formation. We have determined the crystal structure of the isolated C-terminal domain of SpoVT at 1.5 A by experimental phasing techniques and used this model to solve the structure of the full-length SpoVT at 2.6 A by molecular replacement. SpoVT is a tetramer that shows an overall significant distortion mediated by electrostatic interactions. Two monomers dimerize via the highly charged N-terminal domains to form swapped-hairpin beta-barrels. These asymmetric dimers further tetramerize through the formation of mixed helix bundles between their C-terminal domains, which themselves fold as GAF (cGMP-specific and cGMP-stimulated phosphodiesterases, Anabaena adenylate cyclases, and Escherichia coli FhlA) domains. The combination of a swapped-hairpin beta-barrel with a GAF domain represents a novel domain architecture in transcription factors. The occurrence of SpoVT homologs throughout Bacilli and Clostridia demonstrates the ancestral origin of this factor in sporulation.

PMID:
18996130
DOI:
10.1016/j.jmb.2008.10.061
[Indexed for MEDLINE]

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