Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity

ABSTRACT N-glycosylation in Archaea presents aspects of this posttranslational modification not seen in either Eukarya or Bacteria. In the haloarchaeon Haloferax volcanii, the surface (S)-layer glycoprotein can be simultaneously modified by two different N-glycans. Asn-13 and Asn-83 are modified by...

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Autores principales:	Lina Kaminski, Ziqiang Guan, Sophie Yurist-Doutsch, Jerry Eichler
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2013
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/7f3295b480874a52992cc062ec89a116
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spelling	oai:doaj.org-article:7f3295b480874a52992cc062ec89a1162021-11-15T15:42:32ZTwo Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity10.1128/mBio.00716-132150-7511https://doaj.org/article/7f3295b480874a52992cc062ec89a1162013-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00716-13https://doaj.org/toc/2150-7511ABSTRACT N-glycosylation in Archaea presents aspects of this posttranslational modification not seen in either Eukarya or Bacteria. In the haloarchaeon Haloferax volcanii, the surface (S)-layer glycoprotein can be simultaneously modified by two different N-glycans. Asn-13 and Asn-83 are modified by a pentasaccharide, whereas Asn-498 is modified by a tetrasaccharide of distinct composition, with N-glycosylation at this position being related to environmental conditions. Specifically, N-glycosylation of Asn-498 is detected when cells are grown in the presence of 1.75 but not 3.4 M NaCl. While deletion of genes encoding components of the pentasaccharide assembly pathway had no effect on the biosynthesis of the tetrasaccharide bound to Asn-498, deletion of genes within the cluster spanning HVO_2046 to HVO_2061 interfered with the assembly and attachment of the Asn-498-linked tetrasaccharide. Transfer of the “low-salt” tetrasaccharide from the dolichol phosphate carrier upon which it is assembled to S-layer glycoprotein Asn-498 did not require AglB, the oligosaccharyltransferase responsible for pentasaccharide attachment to Asn-13 and Asn-83. Finally, although biogenesis of the low-salt tetrasaccharide is barely discernible upon growth at the elevated salinity, this glycan was readily detected under such conditions in strains deleted of pentasaccharide biosynthesis pathway genes, indicative of cross talk between the two N-glycosylation pathways. IMPORTANCE In the haloarchaeon Haloferax volcanii, originally from the Dead Sea, the pathway responsible for the assembly and attachment of a pentasaccharide to the S-layer glycoprotein, a well-studied glycoprotein in this species, has been described. More recently, it was shown that in response to growth in low salinity, the same glycoprotein is modified by a novel tetrasaccharide. In the present study, numerous components of the pathway used to synthesize this “low-salt” tetrasaccharide are described. As such, this represents the first report of two N-glycosylation pathways able to simultaneously modify a single protein as a function of environmental salinity. Moreover, and to the best of our knowledge, the ability to N-glycosylate the same protein with different and unrelated glycans has not been observed in either Eukarya or Bacteria or indeed beyond the halophilic archaea, for which similar dual modification of the Halobacterium salinarum S-layer glycoprotein was reported.Lina KaminskiZiqiang GuanSophie Yurist-DoutschJerry EichlerAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 4, Iss 6 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Lina Kaminski Ziqiang Guan Sophie Yurist-Doutsch Jerry Eichler Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity
description	ABSTRACT N-glycosylation in Archaea presents aspects of this posttranslational modification not seen in either Eukarya or Bacteria. In the haloarchaeon Haloferax volcanii, the surface (S)-layer glycoprotein can be simultaneously modified by two different N-glycans. Asn-13 and Asn-83 are modified by a pentasaccharide, whereas Asn-498 is modified by a tetrasaccharide of distinct composition, with N-glycosylation at this position being related to environmental conditions. Specifically, N-glycosylation of Asn-498 is detected when cells are grown in the presence of 1.75 but not 3.4 M NaCl. While deletion of genes encoding components of the pentasaccharide assembly pathway had no effect on the biosynthesis of the tetrasaccharide bound to Asn-498, deletion of genes within the cluster spanning HVO_2046 to HVO_2061 interfered with the assembly and attachment of the Asn-498-linked tetrasaccharide. Transfer of the “low-salt” tetrasaccharide from the dolichol phosphate carrier upon which it is assembled to S-layer glycoprotein Asn-498 did not require AglB, the oligosaccharyltransferase responsible for pentasaccharide attachment to Asn-13 and Asn-83. Finally, although biogenesis of the low-salt tetrasaccharide is barely discernible upon growth at the elevated salinity, this glycan was readily detected under such conditions in strains deleted of pentasaccharide biosynthesis pathway genes, indicative of cross talk between the two N-glycosylation pathways. IMPORTANCE In the haloarchaeon Haloferax volcanii, originally from the Dead Sea, the pathway responsible for the assembly and attachment of a pentasaccharide to the S-layer glycoprotein, a well-studied glycoprotein in this species, has been described. More recently, it was shown that in response to growth in low salinity, the same glycoprotein is modified by a novel tetrasaccharide. In the present study, numerous components of the pathway used to synthesize this “low-salt” tetrasaccharide are described. As such, this represents the first report of two N-glycosylation pathways able to simultaneously modify a single protein as a function of environmental salinity. Moreover, and to the best of our knowledge, the ability to N-glycosylate the same protein with different and unrelated glycans has not been observed in either Eukarya or Bacteria or indeed beyond the halophilic archaea, for which similar dual modification of the Halobacterium salinarum S-layer glycoprotein was reported.
format	article
author	Lina Kaminski Ziqiang Guan Sophie Yurist-Doutsch Jerry Eichler
author_facet	Lina Kaminski Ziqiang Guan Sophie Yurist-Doutsch Jerry Eichler
author_sort	Lina Kaminski
title	Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity
title_short	Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity
title_full	Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity
title_fullStr	Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity
title_full_unstemmed	Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity
title_sort	two distinct n-glycosylation pathways process the <named-content content-type="genus-species">haloferax volcanii</named-content> s-layer glycoprotein upon changes in environmental salinity
publisher	American Society for Microbiology
publishDate	2013
url	https://doaj.org/article/7f3295b480874a52992cc062ec89a116
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Two Distinct N-Glycosylation Pathways Process the <named-content content-type="genus-species">Haloferax volcanii</named-content> S-Layer Glycoprotein upon Changes in Environmental Salinity

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