Induction of surfactin production in Bacillus subtilis by gsp, a gene located upstream of the gramicidin S operon in Bacillus brevis
Open Access
- 1 April 1994
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 176 (8) , 2458-2462
- https://doi.org/10.1128/jb.176.8.2458-2462.1994
Abstract
The deduced amino acid sequence of the gsp gene, located upstream of the 5' end of the gramicidin S operon (grs operon) in Bacillus brevis, showed a high degree of similarity to the sfp gene product, which is located downstream of the srfA operon in B. subtilis. The gsp gene complemented in trans a defect in the sfp gene (sfpO) and promoted production of the lipopeptide antibiotic surfactin. The functional homology of Gsp and Sfp and the sequence similarity of these two proteins to EntD suggest that the three proteins represent a new class of proteins involved in peptide secretion, in support of a hypothesis published previously (T. H. Grossman, M. Tuckman, S. Ellestad, and M. S. Osburne, J. Bacteriol. 175:6203-6211, 1993).Keywords
This publication has 21 references indexed in Scilit:
- Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilisMolecular Microbiology, 1993
- Characterization of the srfA locus of Bacillus subtilis: only the valine‐activating domain of srfA is involved in the establishment of genetic competenceMolecular Microbiology, 1993
- Multidomain enzymes involved in peptide synthesisFEBS Letters, 1992
- Identification of putative multifunctional peptide synthetase genes using highly conserved oligonucleotide sequences derived from known synthetasesFEMS Microbiology Letters, 1992
- Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate‐forming enzymesMolecular Microbiology, 1992
- GENETICS OF ENDOSPORE FORMATION IN BACILLUS SUBTILISAnnual Review of Genetics, 1986
- “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein AAnalytical Biochemistry, 1981
- Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymesAnalytical Biochemistry, 1980
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Surfactin, a crystalline peptidelipid surfactant produced by Bacillussubtilis: Isolation, characterization and its inhibition of fibrin clot formationBiochemical and Biophysical Research Communications, 1968