Published:
American Society for Microbiology, 2002
Published in:
Journal of Bacteriology, 184 (2002) 6, Seite 1703-1711
Language:
English
DOI:
10.1128/jb.184.6.1703-1711.2002
ISSN:
0021-9193;
1098-5530
Origination:
Footnote:
Description:
<jats:title>ABSTRACT</jats:title>
<jats:p>
A lantibiotic gene cluster was identified in
<jats:italic>Bacillus subtilis</jats:italic>
A1/3 showing a high degree of homology to the subtilin gene cluster and occupying the same genetic locus as the
<jats:italic>spa</jats:italic>
genes in
<jats:italic>B. subtilis</jats:italic>
ATCC 6633. The gene cluster exhibits diversity with respect to duplication of two subtilin-like genes which are separated by a sequence similar to a portion of a
<jats:italic>lanC</jats:italic>
gene. Matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) analyses of
<jats:italic>B. subtilis</jats:italic>
A1/3 culture extracts confirmed the presence of two lantibiotic-like peptides, ericin S (3,442 Da) and ericin A (2,986 Da). Disruption of the
<jats:italic>lanB</jats:italic>
-homologous gene
<jats:italic>eriB</jats:italic>
resulted in loss of production of both peptides, demonstrating that they are processed in an
<jats:italic>eriB</jats:italic>
-dependent manner. Although precursors of ericins S and A show only 75% of identity, the matured lantibiotic-like peptides reveal highly similar physical properties; separation was only achieved after multistep, reversed-phase high-performance liquid chromatography. Based on Edman and peptidase degradation in combination with MALDI-TOF MS, for ericin S a subtilin-like, lanthionine-bridging pattern is supposed. For ericin A two C-terminal rings are different from the lanthionine pattern of subtilin. Due to only four amino acid exchanges, ericin S and subtilin revealed similar antibiotic activities as well as similar properties in response to heat and protease treatment. For ericin A only minor antibiotic activity was found.
</jats:p>