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J. Biol. Chem., Vol. 278, Issue 23, 20898-20905, June 6, 2003

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Evidence in Support of a Docking Model for the Release of the Transcription Factor ^F from the Antisigma Factor SpoIIAB in Bacillus subtilis^*

Margaret S. Ho, Karen Carniol  and Richard Losick 

From the Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138

Cell-specific activation of the transcription factor ^F during the process of sporulation in Bacillus subtilis is governed by an antisigma factor SpoIIAB and an anti-antisigma factor SpoIIAA. SpoIIAB, which exists as a dimer, binds to ^F in a complex of stoichiometry ^F·SpoIIAB₂. Escape from the complex is mediated by SpoIIAA, which reacts with the complex to cause the release of free ^F. Previous evidence indicated that Arg-20 in SpoIIAB is a contact site for both ^F and SpoIIAA and that contact with ^F is mediated by Arg-20 on only one of the two subunits in the ^F·SpoIIAB₂ complex. Here we report the construction of heterodimers of SpoIIAB in which one subunit is wild type and the other subunit is a mutant for Arg-20. We show that the dissociation constant for the binding of ^F to the heterodimer was similar to that for the wild type, a finding consistent with the idea that ^F contacts Arg-20 on only one of the two subunits. Although SpoIIAA was highly effective in causing the release of ^F from the wild type homodimer, the anti-antisigma factor had little effect on the release of ^F from the heterodimer. This finding is consistent with a model in which SpoIIAA docks on the ^F·SpoIIAB₂ complex, making contact with the subunit in which Arg-20 is not in contact with ^F. SpoIIAB is both an anti-^F factor and a protein kinase that phosphorylates and thereby inactivates SpoIIAA. We show that SpoIIAA effectively displaces ^F from a complex of ^F with a mutant (SpoIIAB^R105A) that is impaired in the kinase function of SpoIIAB. This result shows that SpoIIAA-mediated displacement of ^F from SpoIIAB does not require concomitant phosphorylation of SpoIIAA.

Received for publication, March 5, 2003

^* This work was supported in part by National Institutes of Health Grant GM 18568 (to R. L.). 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.

Supported by predoctoral fellowship from National Science Foundation.

To whom correspondence should be addressed: Dept. of Molecular and Cellular Biology, Harvard University, 16 Divinity Ave., Cambridge, MA 02138. Tel.: 617-495-1774; Fax: 617-496-4642; E-mail: losick{at}mcb.harvard.edu.

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