NMR studies of the sporulation protein SpoIIAA: Implications for the regulation of the transcription factor [sigma]F in Bacillus subtilis

SpoIIAA participates in a four-component mechanism for phosphorylation-dependent transcription control at the outset of sporulation. We report the refinement of the solution structure of SpoIIAA by using the automated iterative NOE assignment method ARIA. To complement the structural data, the protein dynamics were determined by measuring the T^sub 1^, T^sub 2^ and NOE of the backbone ^sup 15^N-nuclei. The refined structure permits a discussion of the structural features that are important for the function of SpoIIAA in the regulation of the sporulation sigma factor σ^sup F^, and for homologous regulatory pathways present in B. subtilis and in other bacilli.[PUBLICATION ABSTRACT]