Tyr-571 is involved in the T7 RNA polymerase binding to its promoter.
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.
Rechinsky
V O
VO
V.A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
Tunitskaya
V L
VL
Dragan
S M
SM
Kostyuk
D A
DA
Kochetkov
S N
SN
D000595:Amino Acid Sequence; D001483:Base Sequence; D004279:DNA, Viral / Q000235:genetics / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D014443:Tyrosine / Q000378:metabolism*; D014764:Viral Proteins
D004279:DNA, Viral; D014764:Viral Proteins; D014443:Tyrosine; C062210:bacteriophage T7 RNA polymerase; D012321:DNA-Directed RNA Polymerases