期刊
ACS CHEMICAL BIOLOGY
卷 17, 期 6, 页码 1513-1523出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.2c00181
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资金
- JSPS KAKENHI (Japan) [15K01823, 19H05648]
- Grants-in-Aid for Scientific Research [19H05648, 15K01823] Funding Source: KAKEN
Ribitol phosphate modifications to the core M3 O-mannosyl glycan play a crucial role in the functional maturation of alpha-dystroglycan. The study reveals that ribitol phosphate transferase catalyzes the transfer of ribitol phosphate and subsequent glycosylation reactions mediated by a series of glycosyltransferases.
Ribitol phosphate modifications to the core M3 O-mannosyl glycan are important for the functional maturation of alpha-dystroglycan. Three sequentially extended partial structures of the core M3 O-mannosyl glycan including a tandem ribitol phosphate were regio- and stereo-selectively synthesized: Rbo5P-3GalNAc beta, Rbo5P-1Rbo5P-3GalNAc beta, and Xyl beta 1-4Rbo5P-1Rbo5P-3GalNAc beta (Rbo5P, d-ribitol-5-phosphate; GalNAc, N-acetyl-d-galactosamine; Xyl, d-xylose). Rbo5P-3GalNAc beta with p-nitrophenyl at the aglycon part served as a substrate for ribitol phosphate transferase (FKRP, fukutin-related protein), and its product was glycosylated by the actions of a series of glycosyltransferases, namely, ribitol xylosyltransferase 1 (RXYLT1), beta 1,4-glucuronyltransferase 1 (B4GAT1), and like-acetyl-glucosaminyltransferase (LARGE). Rbo5P-3GalNAc beta equipped with an alkyne-type aglycon was also active for FKRP. The molecular information obtained on FKRP suggests that Rbo5P-3GalNAc beta derivatives are the minimal units required as the acceptor glycan for Rbo5P transfer and may serve as a precursor for the elongation of the core M3 O-mannosyl glycan.
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