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

C. D'Souza, M. M. Nakano, N. Corbell, P. Zuber

Research output: Contribution to journalArticle

27 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)3502-3510
Number of pages9
JournalJournal of bacteriology
Volume175
Issue number11
DOIs
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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