Change of substrate specificity by polyamines of ribonucleases which hydrolyze ribonucleic acid at linkages attached to pyrimidine nucleotides. |
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| Authors: | K Igarashi H Kumagai Y Watanabe N Toyoda S Hirose |
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| Affiliation: | Faculty of Pharmaceutical Sciences, Chiba University, Yayoi-cho, Chiba, Japan |
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| Abstract: | The activities of ribonucleases (RNase HS and RNase A), which hydrolyze ribonucleic acid at linkages attached to pyrimidine nucleotides were stimulated by polyamines, while the activities of ribonucleases (RNase T1 and RNase M), which attack ribonucleic acid at linkages attached to purine nucleotides were not influenced by polyamines. In the presence of polyamines, the cleavage of C5′-O-P linkages adjacent to cytosine nucleotide was stimulated, while the cleavage of C5′-O-P linkages adjacent to uracil nucleotides was inhibited slightly. The effect of polyamines on the activities of ribonucleases occured through the binding of the polyamines to nucleic acid. |
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| Keywords: | C-3′-P 3′-phosphates of cytidine U-3′-P 3′-phosphates of uridine C-cyclic-P 3′-cyclic phosphates of cytidine U-cyclic-P 2′ 3′-cyclic phosphates uridine |
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