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The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II.

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The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II.

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Title: The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II.
Author: Jeon, Choon Ju.; Yoon, Ho Sup.; Agarwal, Kan.
Copyright year: 1994
Abstract: The eukaryotic transcription factor TFIIS enhances elongation and nascent transcript cleavage activities of RNA polymerase II in a stalled elongation complex. By site-directed mutagenesis, we have demonstrated that invariant residues Asp-261 and Glu-262 of the nucleic acid-binding TFIIS Zn ribbon are critical for stimulation of both elongation and RNA cleavage activities of RNA polymerase II. Substitution of either of these residues inactivates both TFIIS functions, suggesting a related role in both activities. These acidic residues may participate in phosphoryl transfer reactions by a two-metal-ion mechanism in a manner analogous to Klenow fragment. The RNA polymerase II itself may contain a Zn ribbon, in as much as the polymerase's 15-kDa subunit contains a sequence that aligns well with the TFIIS Zn ribbon sequence, including a similarly placed pair of acidic residues.
Subject: DRNTU::Science::Chemistry::Biochemistry.
Type: Conference Paper
Conference name: National Academy of Sciences (1994)
School: School of Biological Sciences
Rights: © 1994 National Academy of Sciences.  This is the author created version of a work that has been peer reviewed and accepted for publication by Proceedings of the National Academy of Sciences , National Academy of Sciences.  It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document.  The published version is available at: http://dx.doi.org/10.1073/pnas.91.19.9106
Version: Accepted version

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