Exploring the N-glycosylation pathway in chlamydomonas reinhardtii unravels novel complex structures
Author
Mathieu-Rivet, Elodie; Scholz, Martin; Arias, Carolina; Dardelle, Flavien; Schulze, Stefan; Le Mauff, François; Teo, Gavin; Hochmal, Ana Karina; Blanco-Rivero, Amaya; Loutelier-Bourhis, Corinne; Kiefer-Meyer, Marie Christine; Fufezan, Christian; Burel, Carole; Lerouge, Patrice; Martínez Díez, Flor; Bardor, Muriel; Hippler, MichaelEntity
UAM. Departamento de BiologíaPublisher
American Society for Biochemistry and Molecular Biology [Society Publisher]; Elsevier [Commercial Publisher]Date
2013-11-01Citation
10.1074/mcp.M113.028191
Molecular & Cellular Proteomics 12.11 (2013): 3160-3183
ISSN
1535-9484 (online)DOI
10.1074/mcp.M113.028191Funded by
Collaborative research conducted by the universities of Rouen (France), Munster (Germany), and Autonoma of Madrid (Spain) was supported by the ANR, PLANT-KBBE 2008 program in the frame of the ALGALGLYCO project. The experiments done at Bioprocessing Technology Institute (BTI, Singapore) were supported by the Biomedical Research Council of A*STAR (Agency for Science, Technology and Research). The collaboration between the University of Rouen (France) and BTI (Singapore) is supported by the MERLION 2011 initiative, project Glyco-TOOLS. This work has also been supported by INSA Rouen, CNRS, Region Haute-Normandie, EFRD (No. 31708), and Labex SynOrg (ANR-11-LABX-0029)Editor's Version
https://doi.org/10.1074/mcp.M113.028191Subjects
mass spectrometry; glycomics; glycosylation; Biología y Biomedicina / BiologíaRights
© 2013 by The American Society for Biochemistry and Molecular Biology, IncEsta obra está bajo una licencia de Creative Commons Reconocimiento-NoComercial-SinObraDerivada 4.0 Internacional.
Abstract
Chlamydomonas reinhardtii is a green unicellular eukaryotic model organism for studying relevant biological and biotechnological questions. The availability of genomic resources and the growing interest in C. reinhardtii as an emerging cell factory for the industrial production of biopharmaceuticals require an in-depth analysis of protein N-glycosylation in this organism. Accordingly, we used a comprehensive approach including genomic, glycomic, and glycoproteomic techniques to unravel the N-glycosylation pathway of C. reinhardtii. Using mass-spectrometry-based approaches, we found that both endogenous soluble and membrane-bound proteins carry predominantly oligomannosides ranging from Man-2 to Man-5. In addition, minor complex N-linked glycans were identified as being composed of partially 6-Omethylated Man-3 to Man-5 carrying one or two xylose residues. These findings were supported by results from a glycoproteomic approach that led to the identification of 86 glycoproteins. Here, a combination of in-source collision- induced dissodiation (CID) for glycan fragmentation followed by mass tag-triggered CID for peptide sequencing and PNGase F treatment of glycopeptides in the presence of 18O-labeled water in conjunction with CID mass spectrometric analyses were employed. In conclusion, our data support the notion that the biosynthesis and maturation of N-linked glycans in the endoplasmic reticulum and Golgi apparatus occur via a GnT I-independent pathway yielding novel complex N-linked glycans that maturate differently from their counterparts in land plants. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc
Files in this item
Google Scholar:Mathieu-Rivet, Elodie
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Scholz, Martin
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Arias, Carolina
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Dardelle, Flavien
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Schulze, Stefan
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Le Mauff, François
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Teo, Gavin
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Hochmal, Ana Karina
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Blanco-Rivero, Amaya
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Loutelier-Bourhis, Corinne
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Kiefer-Meyer, Marie Christine
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Fufezan, Christian
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Burel, Carole
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Lerouge, Patrice
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Martínez Díez, Flor
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Bardor, Muriel
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Hippler, Michael
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