Complementary addressed modification of yeast tRNA1Valwith alkylating derivative of d(pC-G)-A. The positions of the alkylated nucleotides and the course of the alkylation in the complex
Autor: | N.I. Grineva, Galina G. Karpova, T.V. Venkstern, L.M. Kuznetsova, Alexander A. Bayev |
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Rok vydání: | 1977 |
Předmět: |
chemistry.chemical_classification
Alkylating Agents Binding Sites Base pair Stereochemistry RNA Valine Saccharomyces cerevisiae Ribonucleotides Alkylation Biology Kinetics Ribonucleases Reaction rate constant Oligodeoxyribonucleotides RNA Transfer Biochemistry chemistry Reagent Transfer RNA Genetics Nucleic Acid Conformation Spectrophotometry Ultraviolet Nucleotide Binding site |
Zdroj: | Nucleic Acids Research. 4:1609-1632 |
ISSN: | 1362-4962 0305-1048 |
DOI: | 10.1093/nar/4.5.1609 |
Popis: | Yeast tRNA Val 1 alkylation with 2', 3'-O-4-(N-2-chloroethyl-N-methylamino) benzylidene d(pC-G)-A proceeds at 20 degrees - 30 degrees C in the complementary complexes which are formed by d(pC-G)-A greater than RC1 binding to 3 sequences of tRNA Val 1 : psi-C-G58 in the T loop, C-G40 at the 3'-side of the anticodon loop and C-G18 in the D loop. The reaction in the complexes results in A53, I35, and psi 13 alkylation to form beta-/N-methyl-N-(formylphenyl 17 amino/ethyl-tRNA Val 1 with the relative rate constants of the alkylation that are 3 or 2 orders of magnitude higher than that for the alkylation without a complex formation. It is the third nucleotide from the 5'-terminus of the binding site of the modifying agent that is subjected to alkylation in the t RNA Val 1. The course of the alkylation does not depend on the possible base pairing of the 3'-terminal nucleotide of the reagent. The extent of the reagent binding and the relative rate constants of the alkalytion in the complexes indicate the following order of the complex stability: (psi-C-G58) greater than (CO-G40) approximately (C-G18) at 20 degrees and (psi-C-G58) greater than (C-G40) greater than (C-G18) at 30 degrees. |
Databáze: | OpenAIRE |
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