N-linked glycosylation in Archaea: two paths to the same glycan.

Abstract:

:N-linked protein glycosylation occurs in all three branches of life, eukaryotes, bacteria and archaea. The simplest system is that of the bacterium, Campylobacter jejuni, in which a heptasaccharide glycan is added to multiple proteins from a single lipid carrier molecule. In the eukaryotic system a conserved tetradecasaccharide modification is first added to target proteins, but is then modified by trimming and addition of other glycans from additional carrier molecules resulting in a diverse array of glycans of distinct functionality. In the halophilic Archaea from the Dead Sea, Haloferax volcanii, the surface array or S-layer protein is glycosylated with a pentasaccharide. This glycan is synthesized from two separate carrier molecules, one that carries a tetrasaccharide and another that carries the terminal mannose, in a process that is analogous to that of eukaryotes. In this issue of Molecular Microbiology the glycosylation of the S-layer of another halophilic Archaea from the Dead Sea, Haloarcula marismortui is characterized (Calo et al., 2011). This S-layer is glycosylated with the same pentasaccharide as that of Hfx.  volcanii, but the intact pentasaccharide is synthesized on a single carrier molecule in Har. marismortui in a process that more closely resembles that of the bacterial N-linked system.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Guerry P

doi

10.1111/j.1365-2958.2011.07782.x

subject

Has Abstract

pub_date

2011-09-01 00:00:00

pages

1133-5

issue

5

eissn

0950-382X

issn

1365-2958

journal_volume

81

pub_type

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