Open AccessStructural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic
Author(s) -
Schnell Norbert,
Entian KarlDieter,
Götz Friedrich,
Hörner Thomas,
Kellner Roland,
Jung Günther
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03056.x
Subject(s) - lantibiotics , lanthionine , structural gene , peptide sequence , nisin , biology , gene , residue (chemistry) , biochemistry , peptide , protein precursor , amino acid , genetics , bacteria , escherichia coli
Peptide antibiotics containing lanthionine and 3‐methyllanthionine bridges, named lantibiotics [1], are of increasing interest. A new lantibiotic, gallidermin, has been isolated from Staphylococcus gallinarum . Here we report the isolation of its structural gene which we name gdmA . In all lantibiotics so far studied genetically, three peptides can be formally distinguished: (i) the primary translation product, which we call the prepeptide; (ii) the propeptide lacking the leader sequence and (iii) the mature lantibiotic. Unlike the plasmid‐coded epidermin, gdmA is located on the chromosome. The gdmA locus codes for a 52 amino acid residue prepeptide, consisting of an α‐helical leader sequence of hydrophilic character, which is separated from the C‐terminus (propeptide) by a characteristic proteolytic processing site (Pro −2 Arg −1 Ile 1 ). Although pro‐gallidermin