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Bacteriocin ASM1 is an O / S ‐diglycosylated, plasmid‐encoded homologue of glycocin F
Author(s) -
Main Patrick,
Hata Tomomi,
Loo Trevor S.,
Man Petr,
Novak Petr,
Havlíček Vladimír,
Norris Gillian E.,
Patchett Mark L.
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13708
Subject(s) - bacteriocin , plasmid , gene , biology , genome , amino acid , genetics , bacteria
Here, we report on the biochemical characterization of a new glycosylated bacteriocin (glycocin), ASM1, produced by Lactobacillus plantarum A‐1 and analysis of the A‐1 bacteriocinogenic genes. ASM1 is 43 amino acids in length with Ser18‐O‐ and Cys43‐S‐linked N‐acetylglucosamine moieties that are essential for its inhibitory activity. Its only close homologue, glycocin F (GccF), has five amino acid substitutions all residing in the flexible C‐terminal ‘tail’ and a lower IC 50 (0.9 n m ) compared to that of ASM1 (1.5 n m ). Asm / gcc genes share the same organization ( asmH ← → asmABCDE → F ), and the asm genes reside on an 11 905‐bp plasmid dedicated to ASM1 production. The A‐1 genome also harbors a gene encoding a ‘rare’ bactofencin‐type bacteriocin. As more examples of prokaryote S‐GlcNAcylation are discovered, the functions of this modification may be understood.