Related Experiment Video
Updated: Jun 12, 2025

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
N-glycosylation in Archaea - Expanding the process, components and roles of a universal post-translational
Zlata Vershinin1, Marianna Zaretsky1, Jerry Eichler1
1Dept. of Life Sciences, Ben-Gurion University of the Negev, Beersheva, Israel.
Abstract:
While performed by all three domains of life, N-glycosylation in Archaea is less well described than are the parallel eukaryal and bacterial processes. Still, what is known of the archaeal version of this universal post-translational modification reveals numerous seemingly domain-specific traits. Specifically, the biosynthesis of archaeal N-linked glycans relies on distinct pathway steps and components, rare sugars and sugar modifications, as well as unique lipid carriers upon which N-linked glycans are assembled. At the same time, Archaea possess the apparently unique ability to simultaneously modify their glycoproteins with very different N-linked glycans. In addition to these biochemical aspects of archaeal N-glycosylation, such post-translational modification has been found to serve a wide range of roles possibly unique to Archaea, including allowing these microorganisms to not only cope with the harsh physical conditions of the niches they can inhabit but also providing the ability to adapt to transient changes in such environments.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Glycosylation
Glycosylation occurs in...
Proteoglycans
Protein Folding Quality Check in the RER
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Glycocalyx and its Functions

