Exploring the N-glycosylation Pathway in Chlamydomonas reinhardtii Unravels Novel Complex Structures

• DOI: 10.1074/mcp.m113.028191
• Publication Date: 2013-08-03T05:07:01Z
• Authors: Elodie Mathieu-Rivet; Martin Scholz; Carolina Arias; Flavien Dardelle; Stefan Schulze; François Le Mauff; Gavin Teo; Ana Karina Hochmal; Amaya Blanco-Rivero; Corinne Loutelier...; Marie-Christine K...; Christian Fufezan; Carole Burel; Patrice Lerouge; Flor Martinez; Muriel Bardor; Michael Hippler
• Keywords: Chlamydomonas reinhardtii; Glycoproteomics; N-linked glycosylation; Chlamydomonas; Proteome

Chlamydomonas reinhardtii is a green unicellular eukaryotic model organism for studying relevant biological and biotechnological questions. The availability of genomic resources the growing interest in C. as an emerging cell factory industrial production biopharmaceuticals require in-depth analysis protein N-glycosylation this organism. Accordingly, we used comprehensive approach including genomic, glycomic, glycoproteomic techniques to unravel pathway reinhardtii. Using mass-spectrometry-based approaches, found that both endogenous soluble membrane-bound proteins carry predominantly oligomannosides ranging from Man-2 Man-5. In addition, minor complex N-linked glycans were identified being composed partially 6-O-methylated Man-3 Man-5 carrying one or two xylose residues. These findings supported by results led identification 86 glycoproteins. Here, combination in-source collision-induced dissodiation (CID) glycan fragmentation followed mass tag-triggered CID peptide sequencing PNGase F treatment glycopeptides presence (18)O-labeled water conjunction with spectrometric analyses employed. conclusion, our data support notion biosynthesis maturation endoplasmic reticulum Golgi apparatus occur via GnT I-independent yielding novel maturate differently their counterparts land plants.