Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway

Whereas N-glycosylation is a seemingly universal process in Archaea, pathways of N-glycosylation have only been experimentally verified in a mere handful of species. Toward expanding the number of delineated archaeal N-glycosylation pathways, the involvement of the putative Halobacterium salinarum g...

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Autores principales:	Zlata Vershinin, Marianna Zaretsky, Ziqiang Guan, Jerry Eichler
Formato:	article
Lenguaje:	EN
Publicado:	Frontiers Media S.A. 2021
Materias:	archaea archaellin dolichol phosphate Halobacterium salinarum N-glycosylation S-layer glycoprotein Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/47975201b00846939495c1dd0e7a458c
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id	oai:doaj.org-article:47975201b00846939495c1dd0e7a458c
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spelling	oai:doaj.org-article:47975201b00846939495c1dd0e7a458c2021-12-02T10:11:08ZIdentifying Components of a Halobacterium salinarum N-Glycosylation Pathway1664-302X10.3389/fmicb.2021.779599https://doaj.org/article/47975201b00846939495c1dd0e7a458c2021-12-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fmicb.2021.779599/fullhttps://doaj.org/toc/1664-302XWhereas N-glycosylation is a seemingly universal process in Archaea, pathways of N-glycosylation have only been experimentally verified in a mere handful of species. Toward expanding the number of delineated archaeal N-glycosylation pathways, the involvement of the putative Halobacterium salinarum glycosyltransferases VNG1067G, VNG1066C, and VNG1062G in the assembly of an N-linked tetrasaccharide decorating glycoproteins in this species was addressed. Following deletion of each encoding gene, the impact on N-glycosylation of the S-layer glycoprotein and archaellins, major glycoproteins in this organism, was assessed by mass spectrometry. Likewise, the pool of dolichol phosphate, the lipid upon which this glycan is assembled, was also considered in each deletion strain. Finally, the impacts of such deletions were characterized in a series of biochemical, structural and physiological assays. The results revealed that VNG1067G, VNG1066C, and VNG1062G, renamed Agl25, Agl26, and Agl27 according to the nomenclature used for archaeal N-glycosylation pathway components, are responsible for adding the second, third and fourth sugars of the N-linked tetrasaccharide decorating Hbt. salinarum glycoproteins. Moreover, this study demonstrated how compromised N-glycosylation affects various facets of Hbt. salinarum cell behavior, including the transcription of archaellin-encoding genes.Zlata VershininMarianna ZaretskyZiqiang GuanJerry EichlerFrontiers Media S.A.articlearchaeaarchaellindolichol phosphateHalobacterium salinarumN-glycosylationS-layer glycoproteinMicrobiologyQR1-502ENFrontiers in Microbiology, Vol 12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	archaea archaellin dolichol phosphate Halobacterium salinarum N-glycosylation S-layer glycoprotein Microbiology QR1-502
spellingShingle	archaea archaellin dolichol phosphate Halobacterium salinarum N-glycosylation S-layer glycoprotein Microbiology QR1-502 Zlata Vershinin Marianna Zaretsky Ziqiang Guan Jerry Eichler Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway
description	Whereas N-glycosylation is a seemingly universal process in Archaea, pathways of N-glycosylation have only been experimentally verified in a mere handful of species. Toward expanding the number of delineated archaeal N-glycosylation pathways, the involvement of the putative Halobacterium salinarum glycosyltransferases VNG1067G, VNG1066C, and VNG1062G in the assembly of an N-linked tetrasaccharide decorating glycoproteins in this species was addressed. Following deletion of each encoding gene, the impact on N-glycosylation of the S-layer glycoprotein and archaellins, major glycoproteins in this organism, was assessed by mass spectrometry. Likewise, the pool of dolichol phosphate, the lipid upon which this glycan is assembled, was also considered in each deletion strain. Finally, the impacts of such deletions were characterized in a series of biochemical, structural and physiological assays. The results revealed that VNG1067G, VNG1066C, and VNG1062G, renamed Agl25, Agl26, and Agl27 according to the nomenclature used for archaeal N-glycosylation pathway components, are responsible for adding the second, third and fourth sugars of the N-linked tetrasaccharide decorating Hbt. salinarum glycoproteins. Moreover, this study demonstrated how compromised N-glycosylation affects various facets of Hbt. salinarum cell behavior, including the transcription of archaellin-encoding genes.
format	article
author	Zlata Vershinin Marianna Zaretsky Ziqiang Guan Jerry Eichler
author_facet	Zlata Vershinin Marianna Zaretsky Ziqiang Guan Jerry Eichler
author_sort	Zlata Vershinin
title	Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway
title_short	Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway
title_full	Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway
title_fullStr	Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway
title_full_unstemmed	Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway
title_sort	identifying components of a halobacterium salinarum n-glycosylation pathway
publisher	Frontiers Media S.A.
publishDate	2021
url	https://doaj.org/article/47975201b00846939495c1dd0e7a458c
work_keys_str_mv	AT zlatavershinin identifyingcomponentsofahalobacteriumsalinarumnglycosylationpathway AT mariannazaretsky identifyingcomponentsofahalobacteriumsalinarumnglycosylationpathway AT ziqiangguan identifyingcomponentsofahalobacteriumsalinarumnglycosylationpathway AT jerryeichler identifyingcomponentsofahalobacteriumsalinarumnglycosylationpathway
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Identifying Components of a Halobacterium salinarum N-Glycosylation Pathway

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