Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.

In the halophilic archaea Haloferax volcanii, the surface (S)-layer glycoprotein can be modified by two distinct N-linked glycans. The tetrasaccharide attached to S-layer glycoprotein Asn-498 comprises a sulfated hexose, two hexoses and a rhamnose. While Agl11-14 have been implicated in the appearan...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Lina Kaminski, Jerry Eichler
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9253f7d6bc2b41ef80d8fcd49538505e
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:9253f7d6bc2b41ef80d8fcd49538505e
record_format	dspace
spelling	oai:doaj.org-article:9253f7d6bc2b41ef80d8fcd49538505e2021-11-18T08:19:03ZHaloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.1932-620310.1371/journal.pone.0097441https://doaj.org/article/9253f7d6bc2b41ef80d8fcd49538505e2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24831810/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203In the halophilic archaea Haloferax volcanii, the surface (S)-layer glycoprotein can be modified by two distinct N-linked glycans. The tetrasaccharide attached to S-layer glycoprotein Asn-498 comprises a sulfated hexose, two hexoses and a rhamnose. While Agl11-14 have been implicated in the appearance of the terminal rhamnose subunit, the precise roles of these proteins have yet to be defined. Accordingly, a series of in vitro assays conducted with purified Agl11-Agl14 showed these proteins to catalyze the stepwise conversion of glucose-1-phosphate to dTDP-rhamnose, the final sugar of the tetrasaccharide glycan. Specifically, Agl11 is a glucose-1-phosphate thymidylyltransferase, Agl12 is a dTDP-glucose-4,6-dehydratase and Agl13 is a dTDP-4-dehydro-6-deoxy-glucose-3,5-epimerase, while Agl14 is a dTDP-4-dehydrorhamnose reductase. Archaea thus synthesize nucleotide-activated rhamnose by a pathway similar to that employed by Bacteria and distinct from that used by Eukarya and viruses. Moreover, a bioinformatics screen identified homologues of agl11-14 clustered in other archaeal genomes, often as part of an extended gene cluster also containing aglB, encoding the archaeal oligosaccharyltransferase. This points to rhamnose as being a component of N-linked glycans in Archaea other than Hfx. volcanii.Lina KaminskiJerry EichlerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 5, p e97441 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lina Kaminski Jerry Eichler Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.
description	In the halophilic archaea Haloferax volcanii, the surface (S)-layer glycoprotein can be modified by two distinct N-linked glycans. The tetrasaccharide attached to S-layer glycoprotein Asn-498 comprises a sulfated hexose, two hexoses and a rhamnose. While Agl11-14 have been implicated in the appearance of the terminal rhamnose subunit, the precise roles of these proteins have yet to be defined. Accordingly, a series of in vitro assays conducted with purified Agl11-Agl14 showed these proteins to catalyze the stepwise conversion of glucose-1-phosphate to dTDP-rhamnose, the final sugar of the tetrasaccharide glycan. Specifically, Agl11 is a glucose-1-phosphate thymidylyltransferase, Agl12 is a dTDP-glucose-4,6-dehydratase and Agl13 is a dTDP-4-dehydro-6-deoxy-glucose-3,5-epimerase, while Agl14 is a dTDP-4-dehydrorhamnose reductase. Archaea thus synthesize nucleotide-activated rhamnose by a pathway similar to that employed by Bacteria and distinct from that used by Eukarya and viruses. Moreover, a bioinformatics screen identified homologues of agl11-14 clustered in other archaeal genomes, often as part of an extended gene cluster also containing aglB, encoding the archaeal oligosaccharyltransferase. This points to rhamnose as being a component of N-linked glycans in Archaea other than Hfx. volcanii.
format	article
author	Lina Kaminski Jerry Eichler
author_facet	Lina Kaminski Jerry Eichler
author_sort	Lina Kaminski
title	Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.
title_short	Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.
title_full	Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.
title_fullStr	Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.
title_full_unstemmed	Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.
title_sort	haloferax volcanii n-glycosylation: delineating the pathway of dtdp-rhamnose biosynthesis.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/9253f7d6bc2b41ef80d8fcd49538505e
work_keys_str_mv	AT linakaminski haloferaxvolcaniinglycosylationdelineatingthepathwayofdtdprhamnosebiosynthesis AT jerryeichler haloferaxvolcaniinglycosylationdelineatingthepathwayofdtdprhamnosebiosynthesis
_version_	1718421939321569280

Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.

Ejemplares similares