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N-linked glycosylation in Archaea: a structural, functional, and genetic analysis
Ken F Jarrell1, Yan Ding2, Benjamin H Meyer3
1Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada jarrellk@queensu.ca.
Microbiology and Molecular Biology Reviews : MMBR
|May 22, 2014
Summary
Archaea N-glycosylation, a prevalent protein modification, shares commonalities with other domains but has unique features. Recent advances reveal novel archaeal aspects, including unusual lipid carriers and glycan structures.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- N-glycosylation is a widespread posttranslational modification across all domains of life.
- Studying archaeal N-glycosylation was limited by a lack of molecular tools until recent advancements.
Purpose of the Study:
- To review recent progress in understanding archaeal N-glycosylation pathways.
- To highlight unique features of N-glycosylation in Archaea compared to Eukarya and Bacteria.
Main Methods:
- Mass spectrometry for glycan structural analysis.
- Bioinformatic, genetic, biochemical, and enzymatic approaches.
- Focus on model organisms: Haloferax, Methanococcus, and Sulfolobus.
Main Results:
- Archaea N-glycosylation shares some features with Eukarya and Bacteria but possesses unique aspects.
- Unique features include unusual dolichol lipid carriers, diverse linking sugars, novel glycan constituents, and dual N-glycan attachment.
- Archaea can modify N-glycan composition based on growth conditions.
Conclusions:
- Significant progress has been made in characterizing archaeal N-glycosylation.
- Archaea exhibit distinct N-glycosylation mechanisms, expanding our understanding of this fundamental biological process.
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