0536687 - MBÚ 2021 RIV US eng J - Journal Article
Main, P. - Hata, T. - Loo, T. S. - Man, Petr - Novák, Petr - Havlíček, Vladimír - Norris, G. E. - Patchett, M. L.
Bacteriocin ASM1 is an O/S-diglycosylated, plasmid-encoded homologue of glycocin F.
FEBS Letters. Roč. 594, č. 7 (2020), s. 1196-1206. ISSN 0014-5793. E-ISSN 1873-3468
Institutional support: RVO:61388971
Keywords : bacteriocin * plasmid * S-linked glycopeptide bacteriostatic
OECD category: Biochemistry and molecular biology
Impact factor: 4.124, year: 2020
Method of publishing: Limited access
https://febs.onlinelibrary.wiley.com/doi/abs/10.1002/1873-3468.13708

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 IC50 (0.9 nm) compared to that of ASM1 (1.5 nm). 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.
Permanent Link: http://hdl.handle.net/11104/0314424