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Amino-acylation site mutations in amino acid-activating domains of surfactin synthetase: effects on surfactin production and competence development in Bacillus subtilis.

Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, Shreveport 71130-3932.

ABSTRACT

The part of the srfA operon of Bacillus subtilis that contains the region required for competence development is composed of the first four amino acid-activating domains which are responsible for the incorporation of Glu, Leu, D-Leu, and Val into the peptide moiety of the lipopeptide surfactin. Ser-to-Ala substitutions were made in the amino-acylation site of each domain, and their effects on surfactin production and competence development were examined. All of the mutations conferred a surfactin-negative phenotype, supporting the finding that the conserved Ser in the amino-acylation site is required for peptide synthesis. However, none of the mutations affected significantly competence development or the expression of a lacZ fusion to the late competence operon comG. This, coupled with recent findings that only the fourth, Val-activating, domain is required for competence, suggests that some activity, other than amino-acylation and perhaps unrelated to peptide synthesis, possessed by the fourth domain is involved in the role of srfA in regulating competence development.

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• Stachelhaus, T., Marahiel, M. A. (1995). Modular Structure of Peptide Synthetases Revealed by Dissection of the Multifunctional Enzyme GrsA. J. Biol. Chem. 270: 6163-6169 [Abstract] [Full Text]