About: Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins

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About: Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	O-glycosylation is a ubiquitous eukaryotic post-translational modification, whereas early reports of S-linked glycopeptides have never been verified. Prokaryotes also glycosylate proteins, but there are no confirmed examples of sidechain glycosylation in ribosomal antimicrobial polypeptides collectively known as bacteriocins. Here we show that glycocin F, a bacteriocin secreted by Lactobacillus plantarum KW30, is modified by an N-acetylglucosamine beta-O-linked to Ser18, and an N-acetylhexosamine S-linked to C-terminal Cys43. The O-linked N-acetylglucosamine is essential for bacteriostatic activity, and the C-terminus is required for full potency (IC(50) 2 nM). Genomic context analysis identified diverse putative glycopeptide bacteriocins in Firmicutes O-glycosylation is a ubiquitous eukaryotic post-translational modification, whereas early reports of S-linked glycopeptides have never been verified. Prokaryotes also glycosylate proteins, but there are no confirmed examples of sidechain glycosylation in ribosomal antimicrobial polypeptides collectively known as bacteriocins. Here we show that glycocin F, a bacteriocin secreted by Lactobacillus plantarum KW30, is modified by an N-acetylglucosamine beta-O-linked to Ser18, and an N-acetylhexosamine S-linked to C-terminal Cys43. The O-linked N-acetylglucosamine is essential for bacteriostatic activity, and the C-terminus is required for full potency (IC(50) 2 nM). Genomic context analysis identified diverse putative glycopeptide bacteriocins in Firmicutes (en)
Title	Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins (en)
skos:prefLabel	Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins (en)
skos:notation	RIV/61388971:_____/11:00370943!RIV12-AV0-61388971
http://linked.open...avai/predkladatel	Mikrobiologický ústav AV ČR, v.v.i.
http://linked.open...avai/riv/aktivita	Z
http://linked.open...avai/riv/aktivity	Z(AV0Z50200510)
http://linked.open...iv/cisloPeriodika	4
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Man, Petr Havlíček, Vladimír Novák, Petr
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Mikrobiologický ústav AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	192619
http://linked.open...ai/riv/idVysledku	RIV/61388971:_____/11:00370943
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Post-translational modification; Glycosylation; Bacteriocin (en)
http://linked.open.../riv/klicoveSlovo	Bacteriocin Glycosylation Post-translational modification
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[2E1A30AC5A8F]
http://linked.open...i/riv/nazevZdroje	FEBS Letters
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	10 (xsd:int)
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	585
http://linked.open...iv/tvurceVysledku	Man, Petr Novák, Petr Havlíček, Vladimír Loo, T. S. Moore, Ch. H. Norris, G. E. Patchett, M. L. Preston, J. C. Shastri, S. Stepper, J.
http://linked.open...ain/vavai/riv/wos	000287237100011
http://linked.open...n/vavai/riv/zamer	Microorganisms in Research and Biotechnology
issn	0014-5793
number of pages	6 (xsd:int)
http://bibframe.org/vocab/doi	10.1016/j.febslet.2011.01.023
is http://linked.open...avai/riv/vysledek of	Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins

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