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The trans-activation domain of the sporulation response regulator Spo0A revealed by X-ray crystallography

Lewis, R J, Krzywda, S, Brannigan, J A, Turkenburg, J P, Muchova, K, Dodson, E J, Barak, I and Wilkinson, A J (orcid.org/0000-0003-4577-9479) (2000) The trans-activation domain of the sporulation response regulator Spo0A revealed by X-ray crystallography. Molecular Microbiology. pp. 198-212. ISSN 0950-382X

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Sporulation in Bacillus involves the induction of scores of genes in a temporally and spatially co-ordinated programme of cell development. Its initiation is under the control of an expanded two-component signal transduction system termed a phosphorelay. The master control element in the decision to sporulate is the response regulator, Spo0A, which comprises a receiver or phosphoacceptor domain and an effector or transcription activation domain. The receiver domain of Spo0A shares sequence similarity with numerous response regulators, and its structure has been determined in phosphorylated and unphosphorylated forms. However, the effector domain (C-Spo0A) has no detectable sequence similarity to any other protein, and this lack of structural information is an obstacle to understanding how DNA binding and transcription activation are controlled by phosphorylation in Spo0A. Here, we report the crystal structure of C-Spo0A from Bacillus stearothermophilus revealing a single alpha -helical domain comprising six alpha -helices in an unprecedented fold. The structure contains a helix-turn-helix as part of a three alpha -helical bundle reminiscent of the catabolite gene activator protein (CAP), suggesting a mechanism for DNA binding. The residues implicated in forming the sigma (A)-activating region clearly cluster in a flexible segment of the polypeptide on the opposite side of the structure from that predicted to interact with DNA. The structural results are discussed in the context of the rich array of existing mutational data.

Item Type: Article
Copyright, Publisher and Additional Information: © 2000 Blackwell Science Ltd. This is an electronic version of an article published in Molecular Microbiology: complete citation information for the final version of the paper, as published in the print edition of Molecular Microbiology, is available on the Blackwell Synergy online delivery service, accessible via the journal's website at http://www.blackwellpublishing.com/journal.asp?ref=0950-382X or www.blackwell-synergy.com
Institution: The University of York
Academic Units: The University of York > Chemistry (York)
Depositing User: Repository Officer
Date Deposited: 29 Apr 2005
Last Modified: 07 Aug 2016 00:05
Published Version: http://dx.doi.org/10.1046/j.1365-2958.2000.02134.x
Status: Published
Refereed: Yes
URI: http://eprints.whiterose.ac.uk/id/eprint/447

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