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

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Asen I,Djuranovic S,Lupas AN,Zeth K

doi

10.1016/j.jmb.2008.10.061

subject

Has Abstract

pub_date

2009-03-06 00:00:00

pages

962-75

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(08)01363-6

journal_volume

386

pub_type

杂志文章

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