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Journal of Bacteriology, June 1999, p. 3860-3863, Vol. 181, No. 12
Microbiology Unit, Department of
Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom
Received 10 November 1998/Accepted 11 April 1999
SpoIIAA, a phosphorylatable protein, is essential to the regulation
of
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Genotype, Phenotype, and Protein Structure in a Regulator of
Sporulation: Effects of Mutations in the spoIIAA Gene of
Bacillus subtilis

and
F, the first sporulation-specific transcription
factor of Bacillus subtilis. The solution structure of
SpoIIAA has recently been published. Here we examine four mutant
SpoIIAA proteins and correlate their properties with the phenotypes of
the corresponding B. subtilis mutant strains. Two of the
mutations severely disrupted the structure of the protein, a third
greatly diminished the rate of its phosphorylation and abolished
dephosphorylation, and the fourth left phosphorylation unaffected but
reduced the rate of dephosphorylation about 10-fold.
*
Corresponding author. Mailing address: Microbiology
Unit, Department of Biochemistry, University of Oxford, South Parks
Rd., Oxford OX1 3QU, United Kingdom. Phone: 44 1865 275302. Fax: 44 1865 275297. E-mail: mdy{at}bioch.ox.ac.uk.
Present address: Sir William Dunn School of Pathology, University
of Oxford, Oxford OX1 3RE, United Kingdom.
Present address: Philipps-Universität Marburg, Fachbereich
Biologie, Laboratorium für Mikrobiologie, D-35032 Marburg, Germany.
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