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ID 58129
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Oltmanns, Anne Institute of Plant Biology and Biotechnology, University of Münster
Hoepfner, Lara Institute of Plant Biology and Biotechnology, University of Münster
Scholz, Martin Institute of Plant Biology and Biotechnology, University of Münster
Zinzius, Karen Institute of Plant Biology and Biotechnology, University of Münster
Schulze, Stefan Institute of Plant Biology and Biotechnology, University of Münster
Hippler, Michael Institute of Plant Science and Resources, Okayama University
Abstract
Chlamydomonas reinhardtii (C. reinhardtii) N-glycans carry plant typical beta 1,2-core xylose, alpha 1,3-fucose residues, as well as plant atypical terminal beta 1,4-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.
Keywords
C. reinhardtii
N-glycosylation
xylosyltransferase
fucosyltransferase
mass spectrometry
post-translational modification
secretory pathway
Published Date
2020-01-15
Publication Title
Frontiers in Plant Science
Volume
volume10
Publisher
Frontiers Media
Start Page
1686
ISSN
1664-462X
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
Copyright Holders
© 2020 Oltmanns, Hoepfner, Scholz, Zinzius, Schulze and Hippler.
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Related Url
isVersionOf https://doi.org/10.3389/fpls.2019.01686
License
https://creativecommons.org/licenses/by/4.0/