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Science 25 May 1990:
Vol. 248. no. 4958, pp. 1006 - 1009
DOI: 10.1126/science.1693014
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Articles

Science, Vol 248, Issue 4958, 1006-1009
Copyright © 1990 by American Association for the Advancement of Science

articles

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

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

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

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.


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Inter- and Intrasubunit Interactions during the Formation of RNA Polymerase Assembly Intermediate.
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