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      N-Linked Glycans Are Assembled on Highly Reduced Dolichol Phosphate Carriers in the Hyperthermophilic Archaea Pyrococcus furiosus

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          Abstract

          In all three domains of life, N-glycosylation begins with the assembly of glycans on phosphorylated polyisoprenoid carriers. Like eukaryotes, archaea also utilize phosphorylated dolichol for this role, yet whereas the assembled oligosaccharide is transferred to target proteins from dolichol pyrophosphate in eukaryotes, archaeal N-linked glycans characterized to date are derived from a dolichol monophosphate carrier, apart from a single example. In this study, glycan-charged dolichol phosphate from the hyperthermophile Pyrococcus furiosus was identified and structurally characterized. Normal and reverse phase liquid chromatography-electrospray ionization mass spectrometry revealed the existence of dolichol phosphate charged with the heptasaccharide recently described in in vitro studies of N-glycosylation on this species. As with other described archaeal dolichol phosphates, the α- and ω-terminal isoprene subunits of the P. furiosus lipid are saturated, in contrast to eukaryal phosphodolichols that present only a saturated α-position isoprene subunit. Interestingly, an additional 1-4 of the 12-14 isoprene subunits comprising P. furiosus dolichol phosphate are saturated, making this lipid not only the longest archaeal dolichol phosphate described to date but also the most highly saturated.

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          Most cited references 34

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          Terpenoid metabolism.

           R Croteau,  D McGarvey (1995)
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            Protein glycosylation in bacteria: sweeter than ever.

            Investigations into bacterial protein glycosylation continue to progress rapidly. It is now established that bacteria possess both N-linked and O-linked glycosylation pathways that display many commonalities with their eukaryotic and archaeal counterparts as well as some unexpected variations. In bacteria, protein glycosylation is not restricted to pathogens but also exists in commensal organisms such as certain Bacteroides species, and both the N-linked and O-linked glycosylation pathways can modify multiple proteins. Improving our understanding of the intricacies of bacterial protein glycosylation systems should lead to new opportunities to manipulate these pathways in order to engineer glycoproteins with potential value as novel vaccines.
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              Phylogeny and evolution of the Archaea: one hundred genomes later.

              Little more than 30 years since the discovery of the Archaea, over one hundred archaeal genome sequences are now publicly available, of which ∼40% have been released in the last two years. Their analysis provides an increasingly complex picture of archaeal phylogeny and evolution with the proposal of new major phyla, such as the Thaumarchaeota, and important information on the evolution of key central cellular features such as cell division. Insights have been gained into the events and processes in archaeal evolution, with a number of additional and unexpected links to the Eukaryotes revealed. Taken together, these results predict that many more surprises will be found as new archaeal genomes are sequenced. Copyright © 2011 Elsevier Ltd. All rights reserved.
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                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                PLoS ONE
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, CA USA )
                1932-6203
                22 June 2015
                2015
                : 10
                : 6
                Affiliations
                [1 ]Departments of Biology and Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States of America
                [2 ]Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel
                [3 ]Department of Biochemistry, Duke University Medical Center, Durham NC 27710, United States of America
                Weizmann Institute of Science, ISRAEL
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                Conceived and designed the experiments: MC BI JE ZG. Performed the experiments: MC ZG. Analyzed the data: MC BI JE ZG. Contributed reagents/materials/analysis tools: MC BI JE ZG. Wrote the paper: MC BI JE ZG.

                Article
                PONE-D-15-14414
                10.1371/journal.pone.0130482
                4476749
                26098850

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited

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                Figures: 3, Tables: 0, Pages: 11
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                Funding
                This work was supported by the National Institutes of Health (NIH) through grant GM-039334 to B.I. and by the Israel Science Foundation through grant 8/11 to J.E. The mass spectrometry facility in the Department of Biochemistry of the Duke University Medical Center and Z.G. were supported by the NIH through the LIPID MAPS Large Scale Collaborative Grant number GM-069338 to Z.G.
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