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The aim of work was settlement of occurrence of pathogenic fungus Trichosporon cutaneum in diverse ecological environments. Object to investigations farmer river Węgorapa, Supraśl, lakes of complex Mamry and Sejny group, of cultivation ponds in Popielewo and in Poryte Jabłoń a few springs of city Białystok. In investigations one used method of baits to isolated water fungus. Quality of waters determined by physico-chemistry methods. One fixed, that pathogcnic fungus Trichosporon cutaneum stepped out in waters north-east evn Poland on all investigated sites. It was developed in both strong poluted water of lakes and ponds also in good oxygened waters and springs it was too.
Using the fusion of auxotrophic mutant protoplasts, improved Tńchosporon cutaneum hybrids have been obtained. They revealed better, from 15% to 50%, ability to hydrolizę cellulose, and higher, from 23% to 31%, production of biomass in the model medium. They enriched the medium containing a corn coffee extract and not preadapted for yeast cultivation with protein by about 15%.
We have found that heparin has a different effect on Trichosporon cutaneum ribosomal protein phosphorylation by CKI and by CKII. In the presence of heparin, modification of 13 kDa, 19 kDa and 38 kDa proteins catalyzed by CKII was inhibited, while in the case of CKI, in addition to protein of 15 kDa, phosphorylation of 20 kDa and 35 kDa proteins was detected. It was also found that, in the presence of heparin, phosphorylation of P proteins (13 kDa and 38 kDa) by ribosome-bound protein kinases was inhibited. Moreover at the same conditions modification of 40 kDa protein was observed in all four yeast species tested.
Phosphorylation of acidic ribosomal proteins P1/P2-P0 is a common phenomenon in eukaryotic organisms. It was found previously that in Trichosporon cutaneum, un­like in other yeast species, in addition to the two acidic ribosomal proteins, two other proteins of 15 kDa and 19 kDa of the small ribosomal subunit were phosphorylated. Here we describe two protein kinases: CKI and CKII, which are engaged in the modifi­cation of T. cutaneum ribosomal proteins. The acidic ribosomal proteins and the pro­tein of 19 kDa were modified by CKII associated with ribosomes, while the protein of 15 kDa was modified by CKI. Protein kinase CKI was purified from cell-free extract (CKIC) and from ribosomal fraction (CKIR). The molecular mass of CKIC was estab­lished at 33 kDa while that of CKIR at 35-37 kDa. A protein of 40 kDa copurified with CKIR but not CKIC. Heparin significantly in­creased 40 kDa protein phosphorylation level by CKIR. Microsequencing analysis re­vealed the presence of CKI recognition motifs in the N-terminal fragment of the 40 kDa protein.
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