Tyr-571 is involved in the T7 RNA polymerase binding to its promoter

V O Rechinsky; V L Tunitskaya; S M Dragan; D A Kostyuk; S N Kochetkov

doi:10.1016/0014-5793(93)81646-h

Tyr-571 is involved in the T7 RNA polymerase binding to its promoter

FEBS Lett. 1993 Mar 29;320(1):9-12. doi: 10.1016/0014-5793(93)81646-h.

Authors

V O Rechinsky¹, V L Tunitskaya, S M Dragan, D A Kostyuk, S N Kochetkov

Affiliation

¹ V.A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.

PMID: 8462683
DOI: 10.1016/0014-5793(93)81646-h

Abstract

The in vitro studies of three T7 RNA polymerase point mutants suggest that substitutions of Ala and Thr for Pro-563 and of Ser for Tyr-571 have little effect on the enzyme catalytic competence, but result in its inability to utilize the promoter. Both P563A and P563T mutants retain the promoter-binding ability, whereas the promoter affinity of the Y571S mutant drops drastically.

MeSH terms

Amino Acid Sequence
Base Sequence
DNA, Viral / genetics
DNA, Viral / metabolism
DNA-Directed RNA Polymerases / chemistry
DNA-Directed RNA Polymerases / metabolism*
Molecular Sequence Data
Mutagenesis
Promoter Regions, Genetic*
Protein Binding
Sequence Homology, Amino Acid
Tyrosine / metabolism*
Viral Proteins

Substances

DNA, Viral
Viral Proteins
Tyrosine
bacteriophage T7 RNA polymerase
DNA-Directed RNA Polymerases