ID | 61354 |
フルテキストURL | |
著者 |
Xu, Nannan
Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences
Oltmanns, Anne
Institute for Plant Biology and Biotechnology, University of Münster
Zhao, Longsheng
Institute of Integrative Biology, University of Liverpool, Liverpool
Girot, Antoine
Max Planck Institute for Dynamics and Self-Organization (MPIDS)
Karimi, Marzieh
Max Planck Institute for Dynamics and Self-Organization (MPIDS)
Hoepfner, Lara
Institute for Plant Biology and Biotechnology, University of Münsterative Biology, University of Liverpool, Liverpoolnster
Kelterborn, Simon
Institute of Biology, Experimental Biophysics, Humboldt University of Berlin
Scholz, Martin
Institute for Plant Biology and Biotechnology, University of Münster
Beissel, Julia
Institute for Plant Biology and Biotechnology, University of Münster
Hegemann, Peter
Institute of Biology, Experimental Biophysics, Humboldt University of Berlin
Baeumchen, Oliver
Max Planck Institute for Dynamics and Self-Organization (MPIDS)
Liu, Lu-Ning
Institute of Integrative Biology, University of Liverpool, Liverpool
Huang, Kaiyao
Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences
Hippler, Michael
Institute of Plant Science and Resources, Okayama University
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抄録 | For the unicellular alga Chlamydomonas reinhardtii, the presence of N-glycosylated proteins on the surface of two flagella is crucial for both cell-cell interaction during mating and flagellar surface adhesion. However, it is not known whether only the presence or also the composition of N-glycans attached to respective proteins is important for these processes. To this end, we tested several C. reinhardtii insertional mutants and a CRISPR/Cas9 knockout mutant of xylosyltransferase 1A, all possessing altered N-glycan compositions. Taking advantage of atomic force microscopy and micropipette force measurements, our data revealed that reduction in N-glycan complexity impedes the adhesion force required for binding the flagella to surfaces. This results in impaired polystyrene bead binding and transport but not gliding of cells on solid surfaces. Notably, assembly, intraflagellar transport, and protein import into flagella are not affected by altered N-glycosylation. Thus, we conclude that proper N-glycosylation of flagellar proteins is crucial for adhering C. reinhardtii cells onto surfaces, indicating that N-glycans mediate surface adhesion via direct surface contact.
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発行日 | 2020-12-10
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出版物タイトル |
eLife
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巻 | 9巻
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出版者 | eLife Sciences Publications
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開始ページ | e58805
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ISSN | 2050-084X
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資料タイプ |
学術雑誌論文
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言語 |
英語
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OAI-PMH Set |
岡山大学
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著作権者 | © 2020, Xu et al.
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論文のバージョン | publisher
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PubMed ID | |
DOI | |
Web of Science KeyUT | |
関連URL | isVersionOf https://doi.org/10.7554/eLife.58805
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ライセンス | https://creativecommons.org/licenses/by/4.0/
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