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Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis

Author(s)
Larkin, Angelyn; Imperiali, Barbara; Chang, Michelle; Whitworth, Garrett
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Abstract
Asparagine-linked glycosylation is a complex protein modification conserved among all three domains of life. Herein we report the in vitro analysis of N-linked glycosylation from the methanogenic archaeon Methanococcus voltae. Using a suite of synthetic and semisynthetic substrates, we show that AglK initiates N-linked glycosylation in M. voltae through the formation of α-linked dolichyl monophosphate N-acetylglucosamine, which contrasts with the polyprenyl diphosphate intermediates that feature in both eukaryotes and bacteria. Notably, AglK has high sequence homology to dolichyl phosphate β-glucosyltransferases, including Alg5 in eukaryotes, suggesting a common evolutionary origin. The combined action of the first two enzymes, AglK and AglC, afforded an α-linked dolichyl monophosphate glycan that serves as a competent substrate for the archaeal oligosaccharyl transferase AglB. These studies provide what is to our knowledge the first biochemical evidence revealing that, despite the apparent similarity of the overall pathways, there are actually two general strategies to achieve N-linked glycoproteins across the domains of life.
Date issued
2013-04
URI
http://hdl.handle.net/1721.1/96505
Department
Massachusetts Institute of Technology. Department of Biology; Massachusetts Institute of Technology. Department of Chemistry
Journal
Nature Chemical Biology
Publisher
Nature Publishing Group
Citation
Larkin, Angelyn, Michelle M Chang, Garrett E Whitworth, and Barbara Imperiali. “Biochemical Evidence for an Alternate Pathway in N-Linked Glycoprotein Biosynthesis.” Nat Chem Biol 9, no. 6 (April 28, 2013): 367–373.
Version: Author's final manuscript
ISSN
1552-4450
1552-4469

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