Crystal Structure of SpoVT, the Final Modulator of Gene Expression during Spore Development in Bacillus subtilis

JOURNAL OF MOLECULAR BIOLOGY

卷:386

Article

Asen, Iris²  Djuranovic, Sergej¹  Lupas, Andrei N.¹  Zeth, Kornelius¹ 

[1] Max Planck Inst Dev Biol, Dept Prot Evolut, D-72076 Tubingen, Germany

[2] Max Planck Inst Biochem, Dept Membrane Biochem, D-82152 Martinsried, Germany

关键词: SpoVT;    sporulation;    transcription factor;    AbrB;    GAF domain;   

DOI  :  10.1016/j.jmb.2008.10.061

来源: Elsevier

【 摘 要 】

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 angstrom by experimental phasing techniques and used this model to solve the structure of the full-length SpoVT at 2.6 angstrom 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 GAT 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. (C) 2008 Elsevier Ltd. All rights reserved.

【 授权许可】

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