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- W2034994306 abstract "Crystal structures of the complete RNA polymerase I complex are now revealed. The structures link the opening and closing of this enzyme's DNA-binding cleft to the control of transcription. See Articles p.644 & p.650 RNA polymerase I (Pol I) transcribes ribosomal RNA which is critically required for ribosome assembly, and the enzyme is therefore a major determinant of protein biosynthesis and cell growth. Mis-regulation of Pol I has been associated with several types of cancer, and Pol I is an emerging target for anticancer drugs. In this issue of Nature, two groups, working independently, present the X-ray crystal structure of the complete 14-subunit Pol I from yeast, determined at 3.0 Å and 2.8 Å resolution. The basic architecture of Pol I resembles those of Pol II and Pol III, but its DNA-binding cleft adopts a wider conformation than seen in the other RNA polymerases, and other unique features also provide insights into the functional roles of its components." @default.
- W2034994306 created "2016-06-24" @default.
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- W2034994306 date "2013-10-23" @default.
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- W2034994306 title "Pivotal findings for a transcription machine" @default.
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- W2034994306 doi "https://doi.org/10.1038/nature12700" @default.
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