Halobacterial glycoprotein biosynthesis

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      The most complicated situation is present in H. salinarum, in which the S-layer protein is modified with two different N-linked glycans: a repeating unit glycan found at a single site and a sulfated linear oligosaccharide found at 10 sites. The latter, but not the repeating unit glycan, is also found on the archaellins (40). We observed a significant amount of heterogeneity in the N-linked glycans.

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      For a long time, reports on prokaryotic glycoproteins were restricted to a few archaeal and bacterial examples,23,24 and thus, initially, the presence of glycoproteins in prokaryotes was considered a controversial matter. With the investigations of halobacterial S-layer glycoproteins conducted during the late 1970s and 1980s, the occurrence of glycosylated proteins in prokaryotes became generally accepted.15,25,26 These first prokaryotic glycoproteins were shown to have similar types of glycosidic linkages as those found in eukaryotes.

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      A final trait that distinguishes the archaeal structure from bacterial flagella is glycosylation of the major structural proteins, the archaellins. Very early reports on this post-translational modification [36] coupled with the observation that the glycan attachment to archaellins occurred on the external face of the cytoplasmic membrane [37] led the Sumper group to be the first to propose that a novel assembly mechanism, distinct from that used by bacterial flagella, may be employed for the archaeal structure [38]. It appears that post-translational modification of archaellins through an N-linked glycan attachment is widespread in all branches of archaea [39–41].

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