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 journalArticlepeer-review

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 - 1993

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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