Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus

Hayes et al provide a glycosylation site focused analysis of the glycoproteome of two widely utilized B. cenocepacia strains, K56-2 and H111. This team demonstrates that within these glycoproteomes Serine is the sole residue targeted for protein glycosylation and that glycoproteins/glycosylation sit...

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Autores principales:	Andrew J. Hayes, Jessica M. Lewis, Mark R. Davies, Nichollas E. Scott
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/2019ea4ff1db4aeca29f654e783b44e9
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spelling	oai:doaj.org-article:2019ea4ff1db4aeca29f654e783b44e92021-12-02T17:41:17ZBurkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus10.1038/s42003-021-02588-y2399-3642https://doaj.org/article/2019ea4ff1db4aeca29f654e783b44e92021-09-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02588-yhttps://doaj.org/toc/2399-3642Hayes et al provide a glycosylation site focused analysis of the glycoproteome of two widely utilized B. cenocepacia strains, K56-2 and H111. This team demonstrates that within these glycoproteomes Serine is the sole residue targeted for protein glycosylation and that glycoproteins/glycosylation sites are highly conserved across B. cenocepacia isolates.Andrew J. HayesJessica M. LewisMark R. DaviesNichollas E. ScottNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Andrew J. Hayes Jessica M. Lewis Mark R. Davies Nichollas E. Scott Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus
description	Hayes et al provide a glycosylation site focused analysis of the glycoproteome of two widely utilized B. cenocepacia strains, K56-2 and H111. This team demonstrates that within these glycoproteomes Serine is the sole residue targeted for protein glycosylation and that glycoproteins/glycosylation sites are highly conserved across B. cenocepacia isolates.
format	article
author	Andrew J. Hayes Jessica M. Lewis Mark R. Davies Nichollas E. Scott
author_facet	Andrew J. Hayes Jessica M. Lewis Mark R. Davies Nichollas E. Scott
author_sort	Andrew J. Hayes
title	Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus
title_short	Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus
title_full	Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus
title_fullStr	Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus
title_full_unstemmed	Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus
title_sort	burkholderia pgll enzymes are serine preferring oligosaccharyltransferases which target conserved proteins across the burkholderia genus
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2019ea4ff1db4aeca29f654e783b44e9
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Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus

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