Regulation of Mammalian Protein O-Mannosylation PREFERENTIAL AMINO ACID SEQUENCE FOR O-MANNOSE MODIFICATION
作者： Hiroshi Manya , Takehiro Suzuki , Keiko Akasaka-Manya , Hide-Ki Ishida , Mamoru Mizuno
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摘要: O-Mannosyl glycans are important in muscle and brain development. Protein O-mannosyltransferase (POMT) catalyzes the initial step of O-mannosyl glycan biosynthesis. To understand which serine (Ser) threonine (Thr) residues POMT recognizes for mannosylation, we prepared a series synthetic peptides based on mucin-like domain α-dystroglycan (α-DG), one best known O-mannosylated proteins mammals. In α-DG, spans amino acid 316 to 489. Two similar peptide sequences, corresponding 401–420 336–355, respectively, were strongly mannosylated by POMT, whereas other from α-DG various mucin tandem repeat regions poorly mannosylated. Peptides 336–355 contained four six Ser Thr residues, respectively. Substitution Ala or showed that Thr-414 Thr-351 prominently modified O-mannosylation. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry Edman degradation analysis indicated was residue most O-mannosylation occurred sequentially rather than at random. Based these results, propose preferred sequence mammalian O-mannose modification.
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