Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 411, Issue 4, Pages 721-725Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.07.012
Keywords
Walker-Warburg syndrome; Muscular dystrophy; Glycosyltransferase; Protein O-mannosyltransferase
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Funding
- Japan Society for the Promotion of Science [20370053]
- Intramural Research Grant for Neurological and Psychiatric Disorders of NCNP [23-5]
- Ministry of Health [H22-021]
- Naito Foundation
- Research Foundation for Pharmaceutical Sciences
- Grants-in-Aid for Scientific Research [20370053] Funding Source: KAKEN
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Protein O-mannosyltransferase 1 (POMT1) and its homolog, POMT2, are responsible for the catalysis of the first step in O-mannosyl glycan synthesis. Mutations in their genes are associated with a type of congenital muscular dystrophy called Walker-Warburg syndrome. Arg(64), Glu(78) and Arg(138) in the N-terminus region of ScPmt1p, a POMT homolog in Saccharomyces cerevisiae, are important for transferase activity. Arg(138) is also essential for complex formation with ScPmt2p. Here we examined the effects of replacing the corresponding residues in human POMT1 and POMT2 with Ala on complex formation and enzymatic activity. The human POMT1 mutants lost almost all transferase activity while the POMT2 mutants retained enzymatic activity. Neither mutant lost its ability to form complexes with the native counter component. These results indicate that ScPmtps and human POMTs have different mechanisms of complex formation. They also suggest that human POMT1 and POMT2 have discrete functions since the effect of amino acid substitutions on enzymatic activity are different. (C) 2011 Elsevier Inc. All rights reserved.
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