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, Michiko Nakano, N. Corbell, Peter Zuber

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27 Citations (Scopus)

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
StatePublished - 1993
Externally publishedYes

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Aminoacylation
Bacillus subtilis
Mental Competency
Amino Acids
Mutation
Operon
Peptides
Lipopeptides
surfactin synthetase
Phenotype

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

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title = "Amino-acylation site mutations in amino acid-activating domains of surfactin synthetase: Effects on surfactin production and competence development in Bacillus subtilis",
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.",
author = "C. D'Souza and Michiko Nakano and N. Corbell and Peter Zuber",
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TY - JOUR

T1 - Amino-acylation site mutations in amino acid-activating domains of surfactin synthetase

T2 - Effects on surfactin production and competence development in Bacillus subtilis

AU - D'Souza, C.

AU - Nakano, Michiko

AU - Corbell, N.

AU - Zuber, Peter

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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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