Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea

Mehtap Abu-Qarn, Jerry Eichler, Nathan Sharon

Research output: Contribution to journalReview articlepeer-review

148 Scopus citations


Of the many post-translational modifications proteins can undergo, glycosylation is the most prevalent and the most diverse. Today, it is clear that both N-glycosylation and O-glycosylation, once believed to be restricted to eukaryotes, also transpire in Bacteria and Archaea. Indeed, prokaryotic glycoproteins rely on a wider variety of monosaccharide constituents than do those of eukaryotes. In recent years, substantial progress in describing the enzymes involved in bacterial and archaeal glycosylation pathways has been made. It is becoming clear that enhanced knowledge of bacterial glycosylation enzymes may be of therapeutic value, while the demonstrated ability to introduce bacterial glycosylation genes into Escherichia coli represents a major step forward in glyco-engineering. A better understanding of archaeal protein glycosylation provides insight into this post-translational modification across evolution as well as protein processing under extreme conditions. Here, we discuss new structural and biosynthetic findings related to prokaryotic protein glycosylation, until recently a neglected topic.

Original languageEnglish
Pages (from-to)544-550
Number of pages7
JournalCurrent Opinion in Structural Biology
Issue number5
StatePublished - 1 Oct 2008

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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