Pep5, a new lantibiotic: structural gene isolation and prepeptide sequence

A wobbled 14-mer oligonucleotide was derived from the amino acid sequence of the 34-residue propeptide of the lantibiotic Pep5 (Kellner et al. 1989). Using this hybridization probe, the structural gene of Pep5, pepA, was located on the 18.6 kbp plasmid pED503. The nucleotide sequence of pepA codes f...

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Bibliographic Details
Published in:	Archives of microbiology Vol. 152; no. 1; pp. 16 - 19
Main Authors:	KALETTA, C, ENTIAN, K.-D, KELLNER, R, JUNG, G, REIS, M, SAHL, H.-G
Format:	Journal Article
Language:	English
Published:	Heidelberg Springer 01-06-1989 Berlin
Subjects:	Amino Acid Sequence Anti-Bacterial Agents - analysis Anti-Bacterial Agents - biosynthesis Bacteriocins Bacteriology Base Sequence Biological and medical sciences Blotting, Southern Cloning, Molecular Electrophoresis, Agar Gel Fundamental and applied biological sciences. Psychology Genes Genes, Bacterial Genetics lantibiotic Pep5 Microbiology Molecular Sequence Data Nucleic Acid Hybridization nucleotide sequence oligonucleotides Peptide Biosynthesis Peptides - analysis Peptides - genetics Plasmids Protein Precursors - analysis Protein Precursors - genetics Protein Processing, Post-Translational Staphylococcus epidermidis - genetics Nucleotide sequence Posttranslational modification Plasmid Antibiotic Staphylococcus epidermidis Complementary DNA Gene Restriction map Bacteria Micrococcales Isolation Micrococcaceae Southern blotting Aminoacid sequence
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Summary:	A wobbled 14-mer oligonucleotide was derived from the amino acid sequence of the 34-residue propeptide of the lantibiotic Pep5 (Kellner et al. 1989). Using this hybridization probe, the structural gene of Pep5, pepA, was located on the 18.6 kbp plasmid pED503. The nucleotide sequence of pepA codes for a prepeptide with 60 residues and proves that Pep5 is ribosomally synthesized. The N-terminus of the prepeptide has a high alpha-helix probability and a characteristic proteolytic cleavage site precedes the C-terminal 34-residue propeptide. Our present theory is that maturation of Pep5 involves (a) enzymic conversion of Thr, Ser and Cys into dehydrated amino acids and sulfide bridges, (b) membrane translocation and cleavage of the modified prepeptide.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0302-8933 1432-072X
DOI:	10.1007/bf00447005