Crystal structures of the ADP and ATP bound forms of the Bacillus anti-σ factor SpoIIAB in complex with the anti-anti-σ SpoIIAA

Shoko Masuda, Katsuhiko S. Murakami, Sheng Wang, C. Anders Olson, Jill Donigian, Fred Leon, Seth A. Darst, Elizabeth A. Campbell

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

Cell type-specific transcription during Bacillus sporulation is established by σF, the activity of which is controlled by a regulatory circuit involving the anti-σ factor and serine kinase SpoIIAB, and the anti-anti-σ SpoIIAA. When ATP is present in the nucleotide-binding site of SpoIIAB, SpoIIAA is phosphorylated, followed by dissociation. The nucleotide-binding site of SpoIIAB is left bound to ADP. SpoIIAB(ADP) can bind an unphosphorylated molecule of SpoIIAA as a stable binding partner. Thus, in this circuit, SpoIIAA plays a dual role as a substrate of the SpoIIAB kinase activity, as well as a tight binding inhibitor. Crystal structures of both the pre-phosphorylation complex and the inhibitory complex, SpoIIAB(ATP) and SpoIIAB(ADP) bound to SpoIIAA, respectively, have been determined. The structural differences between the two forms are subtle and confined to interactions with the phosphoryl groups of the nucleotides. The structures reveal details of the SpoIIAA:SpoIIAB interactions and how phosphorylated SpoIIAA dissociates from SpoIIAB(ADP). Finally, the results confirm and expand upon the docking model for SpoIIAA function as an anti-anti-σ in releasing σF from SpoIIAB.

Original languageEnglish (US)
Pages (from-to)941-956
Number of pages16
JournalJournal of Molecular Biology
Volume340
Issue number5
DOIs
StatePublished - Jul 23 2004

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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