Affordable Access

deepdyve-link
Publisher Website

Novel Insights Into N- Glycan Fucosylation and Core Xylosylation in C. reinhardtii

Authors
  • Oltmanns, Anne1
  • Hoepfner, Lara1
  • Scholz, Martin1
  • Zinzius, Karen1
  • Schulze, Stefan1, 2
  • Hippler, Michael1, 3
  • 1 Institute of Plant Biology and Biotechnology, University of Münster, Münster , (Germany)
  • 2 Department of Biology, University of Pennsylvania, Philadelphia, PA , (United States)
  • 3 Institute of Plant Science and Resources, Okayama University, Okayama , (Japan)
Type
Published Article
Journal
Frontiers in Plant Science
Publisher
Frontiers Media SA
Publication Date
Jan 15, 2020
Volume
10
Identifiers
DOI: 10.3389/fpls.2019.01686
PMID: 32010168
PMCID: PMC6974686
Source
PubMed Central
Keywords
License
Unknown

Abstract

Chlamydomonas reinhardtii (C. reinhardtii) N- glycans carry plant typical β1,2-core xylose, α1,3-fucose residues, as well as plant atypical terminal β1,4-xylose and methylated mannoses. In a recent study, XylT1A was shown to act as core xylosyltransferase, whereby its action was of importance for an inhibition of excessive Man1A dependent trimming. N- Glycans found in a XylT1A/Man1A double mutant carried core xylose residues, suggesting the existence of a second core xylosyltransferase in C. reinhardtii . To further elucidate enzymes important for N -glycosylation, novel single knockdown mutants of candidate genes involved in the N -glycosylation pathway were characterized. In addition, double, triple, and quadruple mutants affecting already known N -glycosylation pathway genes were generated. By characterizing N -glycan compositions of intact N -glycopeptides from these mutant strains by mass spectrometry, a candidate gene encoding for a second putative core xylosyltransferase (XylT1B) was identified. Additionally, the role of a putative fucosyltransferase was revealed. Mutant strains with knockdown of both xylosyltransferases and the fucosyltransferase resulted in the formation of N- glycans with strongly diminished core modifications. Thus, the mutant strains generated will pave the way for further investigations on how single N- glycan core epitopes modulate protein function in C. reinhardtii .

Report this publication

Statistics

Seen <100 times