| Autor: |
Maksimova, Tatyana G., Mustayev, Arkady A., Zaychikov, Evgeny F., Lyakhov, Dmitry L., Tunitskaya, Vera L., Akbarov, Akhror Kh., Luchin, Sergei V., Rechinsky, Vladimir O., Chernov, Boris K., Kochetkov, Sergei N. |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 2/14/91, Vol. 195 Issue 3, p841-847, 7p |
| Abstrakt: |
A highly selective affinity labeling of T7 RNA polymerase with the o-formylphenyl ester of GMP and [α-32P]UTP was carried out. The site of the labeling was located using limited cleavages with hydroxylamine, bromine, N-chlorosuccinimide and cyanogene bromide and was identified as the Lys631 residue. Site-directed mutagenesis using synthetic oligonucleotides was used to substitute Lys631 by a Gly, Leu or Arg residue. Kinetic studies of the purified mutant enzymes showed alterations of their polymerizing activity. For the Lys → Gly mutant enzyme, anomalous template binding was observed. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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