A glycopeptide regulating stem cell fate in Arabidopsis thaliana

• Published in: Nature chemical biology Vol. 5; no. 8; pp. 578 - 580
• Main Authors: Matsubayashi, Yoshikatsu, Ohyama, Kentaro, Shinohara, Hidefumi, Ogawa-Ohnishi, Mari
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.08.2009; Nature Publishing Group
• Subjects: Amino Acid Sequence; Arabidopsis - growth & development; Arabidopsis - metabolism; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - genetics; Arabidopsis Proteins - physiology; Biochemical Engineering; Biochemistry; Bioorganic Chemistry; brief-communication; Cell Biology; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Chromatography, Liquid; Gene expression; Genes, Plant; Glycopeptides - chemistry; Glycopeptides - genetics; Glycopeptides - physiology; Mass Spectrometry; Meristem - growth & development; Meristem - metabolism; Molecular Sequence Data; Nanotechnology; Peptides; Plant Shoots - growth & development; Plant Shoots - metabolism; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases; Receptor Protein-Tyrosine Kinases - chemistry; Receptor Protein-Tyrosine Kinases - genetics; Receptor Protein-Tyrosine Kinases - physiology; Stem cells
• ISSN: 1552-4450; 1552-4469
• DOI: 10.1038/nchembio.182

The secreted peptide gene CLAVATA3 (CLV3) regulates stem cell fate in the shoot apical meristem in Arabidopsis thaliana plants, but the molecular structure of the active mature CLV3 peptide is controversial. Here, using nano-LC-MS/MS analysis of apoplastic peptides of A. thaliana plants overexpressing CLV3, we show that CLV3 is a 13-amino-acid arabinosylated glycopeptide. Post-translational arabinosylation of CLV3 is critical for its biological activity and high-affinity binding to its receptor CLV1.