Biosynthesis of glycoproteins in the pathogenic fungus Candida albicans: Activation of dolichol phosphate mannose synthase by cAMP-mediated protein phosphorylation |
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| Authors: | Blanca L. Arroyo-Flores Carlos Calvo-Méndez Arturo Flores-Carreón Everardo López-Romero |
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| Affiliation: | 1. Department of Internal Medicine, Infectious Diseases Division, Washington University, School of Medicine Campus Box 8051, 660 S. Euclid Ave., St. Louis Missouri 63110-1093 USA. Tel.: +1 40 61 35 18; fax: +1 40 61 34 19;2. Laboratorio de Inmunología de Hongos, Depto. de Microbiología y Parasitología, Facultad de Medicina, UNAM Cd. Universitaria 04510 México, D.F. Tel.:/fax: +52 555 56-23-24-62;3. Lille-2 University Hospital Center and Ecology of Parasitism, Institute Pasteur of Lille 1, rue du Prof-Calmette - BP245 59019 Lille cedex (France) Tel.: +33 3 20 87 71 55; fax: +33 3 20 87 72 24 |
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| Abstract: | Following incubation with ATP and a cAMP-dependent protein kinase under optimal conditions of lipid acceptor, phospholipid and metal ion requirements, the transfer activity of partially purified dolichol phosphate mannose synthase (DPMS) increased about 60% and this activation correlated with a 50% increase in Vmax with no alteration in the apparent Km for GDP-Manose. Phosphorylation with [γ-32P]ATP resulted in the labeling of several polypeptides, one of which exhibited the molecular weight of the enzyme (30 kDa) and was also recognized using a specific anti-DPMS monoclonal antibody. This and the fact that the phosphate label could be removed by an alkaline phosphatase indicate that Candida DPMS may be regulated by phosphorylation–dephosphorylation, a mechanism that has been proposed for the enzyme in other organisms. |
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