Phosphorylation of yeast ribosomal proteins by CKI and CKII in the presence of heparin.
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.
Wojda
I
I
Department of Molecular Biology, Institute of Microbiology and Biotechnology, Maria Curie-Skłodowska University, Lublin, Poland.
Cytryńska
M
M
Frajnt
M
M
Jakubowicz
T
T
D047390:Casein Kinase II; D047388:Casein Kinases; D006493:Heparin / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D014250:Trichosporon / Q000378:metabolism*
D012269:Ribosomal Proteins; D006493:Heparin; D011494:Protein Kinases; D047390:Casein Kinase II; D047388:Casein Kinases; D017346:Protein Serine-Threonine Kinases