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Biochem Soc Trans. 2013 Feb 1;41(1):384-92. doi: 10.1042/BST20120296.

Hot and sweet: protein glycosylation in Crenarchaeota.

Author information

1
Molecular Biology of Archaea, Max-Planck Institute for terrestrial Microbiology, Karl-von-Frisch-Strasse 10, 35043 Marburg, Germany.

Erratum in

  • Biochem Soc Trans. 2013 Apr;41(2):695.

Abstract

Every living cell is covered with a dense and complex array of covalently attached sugars or sugar chains. The majority of these glycans are linked to proteins via the so-called glycosylation process. Protein glycosylation is found in all three domains of life: Eukarya, Bacteria and Archaea. However, on the basis of the limit in analytic tools for glycobiology and genetics in Archaea, only in the last few years has research on archaeal glycosylation pathways started mainly in the Euryarchaeota Haloferax volcanii, Methanocaldococcus maripaludis and Methanococcus voltae. Recently, major steps of the crenarchaeal glycosylation process of the thermoacidophilic archaeon Sulfolobus acidocaldarius have been described. The present review summarizes the proposed N-glycosylation pathway of S. acidocaldarius, describing the phenotypes of the mutants disrupted in N-glycan biosynthesis as well as giving insights into the archaeal O-linked and glycosylphosphatidylinositol anchor glycosylation process.

PMID:
23356316
DOI:
10.1042/BST20120296
[Indexed for MEDLINE]

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