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Blocking of the initiation-to-elongation transition by a transdominant RNA polymerase mutation.

作者信息

Kashlev M, Lee J, Zalenskaya K, Nikiforov V, Goldfarb A

机构信息

Institute of Molecular Genetics, U.S.S.R. Academy of Sciences, Moscow.

出版信息

Science. 1990 May 25;248(4958):1006-9. doi: 10.1126/science.1693014.

DOI:10.1126/science.1693014
PMID:1693014
Abstract

RNA polymerase, the principal enzyme of gene expression, possesses structural features conserved in evolution. A substitution of an evolutionarily invariant amino acid (Lys1065----Arg) in the beta subunit of Escherichia coli RNA polymerase apparently disrupts its catalytic center. The mutant protein inhibited cell growth when expressed from an inducible promoter. The assembled holoenzyme carrying the mutant subunit formed stable promoter complexes that continuously synthesized promoter-specific dinucleotides but that did not enter the elongation step. The mutant polymerase inhibited transcription by blocking the access of the wild-type enzyme to promoters.

摘要

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