title: Tyr-571 is involved in the T7 RNA polymerase binding to its promoter.
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.
authors: V.A. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
authors: V O
authors: VO
authors: Rechinsky
authors: V L
authors: VL
authors: Tunitskaya
authors: S M
authors: SM
authors: Dragan
authors: D A
authors: DA
authors: Kostyuk
authors: S N
authors: SN
authors: Kochetkov
mesh_terms: 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
chemical_list: D004279:DNA, Viral; D014764:Viral Proteins; D014443:Tyrosine; C062210:bacteriophage T7 RNA polymerase; D012321:DNA-Directed RNA Polymerases