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J. Biol. Chem., Vol. 280, Issue 43, 36214-36220, October 28, 2005

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The Structure of Bypass of Forespore C, an Intercompartmental Signaling Factor during Sporulation in Bacillus^*

Hayley M. Patterson1, James A. Brannigan2, Simon M. Cutting, Keith S. Wilson, Anthony J. Wilkinson3, Eiso AB¶, Tammo Diercks¶, Rob N. de Jong¶, Vincent Truffault¶4, Gert E. Folkers¶, and Robert Kaptein¶

From the Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom, School of Biological Sciences, Royal Holloway University of London, Egham, Surrey, TW20 0EX, United Kingdom, and ^¶Bijvoet Center, NMR Department, Utrecht University, 3584 CH Utrecht, The Netherlands

Sporulation in Bacillus subtilis begins with an asymmetric cell division giving rise to smaller forespore and larger mother cell compartments. Different programs of gene expression are subsequently directed by compartment-specific RNA polymerase -factors. In the final stages, spore coat proteins are synthesized in the mother cell under the control of RNA polymerase containing ^K, (E^K). ^K is synthesized as an inactive zymogen, pro-^K, which is activated by proteolytic cleavage. Processing of pro-^K is performed by SpoIVFB, a metalloprotease that resides in a complex with SpoIVFA and bypass of forespore (Bof)A in the outer forespore membrane. Ensuring coordination of events taking place in the two compartments, pro-^K processing in the mother cell is delayed until appropriate signals are received from the forespore. Cell-cell signaling is mediated by SpoIVB and BofC, which are expressed in the forespore and secreted to the intercompartmental space where they regulate pro-^K processing by mechanisms that are not yet fully understood. Here we present the three-dimensional structure of BofC determined by solution state NMR. BofC is a monomer made up of two domains. The N-terminal domain, containing a four-stranded -sheet onto one face of which an -helix is packed, closely resembles the third immunoglobulin-binding domain of protein G from Streptococcus. The C-terminal domain contains a three-stranded -sheet and three -helices in a novel domain topology. The sequence connecting the domains contains a conserved DISP motif to which mutations that affect BofC activity map. Possible roles for BofC in the ^K checkpoint are discussed in the light of sequence and structure comparisons.

Received for publication, June 24, 2005

^* The work described here was funded by the European Commission as Structural Proteomics in Europe, Contract QLG2-CT-2002-00988, under the program "Quality of Life and Management of Living Resources." The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2 and Table S1. The atomic coordinates and structure factors (code 2BW2) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

¹ Funded by a Biotechnology and Biological Sciences Research Council studentship.

² Funded by the Wellcome Trust.

⁴ Present address: Max Planck Institute for Developmental Biology, Dept. of Protein Evolution, Spemannstr. 35, 72076 Tübingen, Germany.

³ To whom correspondence should be addressed. Tel.: 44-1904-328261; Fax: 44-1904-328266; E-mail: ajw{at}ysbl.york.ac.uk.

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