Biosynthesis of O-N-acetylglucosamine-linked glycans in Trypanosoma cruzi - Characterization of the novel uridine diphospho-N-acetylglucosamine : polypeptide-N-acetylglucosaminyltransferase- catalyzing formation of N-acetylglucosamine alpha 1 -> O-threonine

Biosynthesis of O-N-acetylglucosamine-linked glycans in Trypanosoma cruzi - Characterization of the novel uridine diphospho-N-acetylglucosamine : polypeptide-N-acetylglucosaminyltransferase- catalyzing formation of N-acetylglucosamine alpha 1 -> O-threonine

Autor Previato, J. O. Google Scholar
Sola-Penna, M. Google Scholar
Agrellos, O. A. Google Scholar
Jones, C. Google Scholar
Oeltmann, T. Google Scholar
Travassos, Luiz Rodolpho Autor UNIFESP Google Scholar
Mendonca-Previato, L. Google Scholar
Instituição Universidade Federal do Rio de Janeiro (UFRJ)
Natl Inst Biol Stand & Controls
Vanderbilt Univ
Universidade Federal de São Paulo (UNIFESP)
Resumo In this study, we have characterized the activity of a uridine diphospho-N-acetylglucosamine:polypeptide-alpha-N-acetylglucosaminyltransferase (O-alpha-GlcNAc-transferase) from Trypanosoma cruzi. the activity is present in microsomal membranes and is responsible for the addition of O-linked alpha-N-acetylglucosamine to cell surface proteins. This preparation adds N-acetylglucosamine to a synthetic peptide KPPTTTTTTTTKPP containing the consensus threonine-rich dodecapeptide encoded by T. cruzi MUC gene (Di Noia, J. M., Sanchez D. O., and Frasch, A. C. C. (1995) J. Biol. Chem. 270, 24146-24149). Incorporation of N-[H-3]acetylglucosamine is linearly dependent on incubation time and concentration of enzyme and substrate. the transferase activity has an optimal pH of 7.5-8.5, requires Mn2+, is unaffected by tunicamycin or amphomycin, and is strongly inhibited by UDP, the optimized synthetic peptide acceptor for the cytosolic O-GlcNAc-transferase (YSDSPSTST) (Haltiwanger, R. S., Holt, G. D., and Hart, G. W. (1990) J. Biol. Chem. 265, 2563-2568) is not a substrate for this enzyme. the glycosylated KPPTTTTTTTTKPP product is susceptible to base-catalyzed beta-elimination, and the presence of N-acetylglucosamine beta-linked to threonine is supported by enzymatic digestion and nuclear magnetic resonance data. These results describe a unique biosynthetic pathway for T. cruzi surface mucin-like molecules, with potential chemotherapeutic implications.
Idioma Inglês
Data de publicação 1998-06-12
Publicado em Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 273, n. 24, p. 14982-14988, 1998.
ISSN 0021-9258 (Sherpa/Romeo, fator de impacto)
Publicador Amer Soc Biochemistry Molecular Biology Inc
Extensão 14982-14988
Fonte http://dx.doi.org/10.1074/jbc.273.24.14982
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:000074160400047
Endereço permanente http://repositorio.unifesp.br/handle/11600/25912

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