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

FEBS Letters

Dragan, S.M.¹  Tunitskaya, V.L.¹  Kostyuk, D.A.¹  Rechinsky, V.O.¹  Kochetkov, S.N.¹ 

[1] V.A. Engelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russian Federation

关键词: Bacteriophage T7;    RNA polymerase;    Mutagenesis;    RNA polymerase promoter interaction;    T7 RNAP;    bacteriophage T7 DNA-dependent RNA polymerase;    w.t;    wild type;    BSA;    bovine scrum albumin;   

DOI  :  10.1016/0014-5793(93)81646-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown