Mannosyl-phospho-dolichol synthase from Trichoderma reesei is activated by protein kinase dependent phosphorylation in vitro
1991
Kruszewska, J. | Palamarczyk, G. | Kubicek, C.P.
Preincubation of microsomes from Trichoderma reesei QM 9414 with the catalytic subunit of cyclic AMP dependent protein kinase from bovine heart resulted in increased activity of the mannosylphospho-dolichol synthase (EC 2.4.1.83, 'Dol-P-Man synthase') present in the membranes. This effect decreased upon subsequent treatment of the microsomes with alkaline phosphatase. SDS-PAGE of microsomal proteins indicated the presence of a strong band at 32 kDa, which corresponds to the size of yeast Dol-P-Man synthase. Fluorography of microsomal proteins, after incubation with [gamma-32P]ATP and protein kinase, revealed the incorporation of 32P into this 32-kDa as well as several other microsomal proteins. Dol-P-Man synthase activity, assayed at various times of growth, correlated with the rise and fall of the cyclic AMP pool in T reesei. Addition of extracellular dibutyryl cyclic AMP and theophyllin, however, did not elevate the internal cyclic AMP pool in the fungus, and did not cause an effect on Dol-P-Man synthase activity.
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