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

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 ar...

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Main Authors: Jeon, Choon Ju, Yoon, Ho Sup, Agarwal, Kan
Other Authors: School of Biological Sciences
Format: Conference or Workshop Item
Language:English
Published: 2012
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Online Access:https://hdl.handle.net/10356/94050
http://hdl.handle.net/10220/7484
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spelling sg-ntu-dr.10356-940502023-02-28T16:54:57Z The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II Jeon, Choon Ju Yoon, Ho Sup Agarwal, Kan School of Biological Sciences National Academy of Sciences (1994) DRNTU::Science::Chemistry::Biochemistry 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. Accepted version 2012-01-26T08:17:57Z 2019-12-06T18:49:57Z 2012-01-26T08:17:57Z 2019-12-06T18:49:57Z 1994 1994 Conference Paper Jeon, C. J., Yoon, H. S. & Agarwal, K. (1994). The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II. Proceedings of the National Academy of Sciences, pp.9106–9110. https://hdl.handle.net/10356/94050 http://hdl.handle.net/10220/7484 10.1073/pnas.91.19.9106 en © 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 application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Chemistry::Biochemistry
spellingShingle DRNTU::Science::Chemistry::Biochemistry
Jeon, Choon Ju
Yoon, Ho Sup
Agarwal, Kan
The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Jeon, Choon Ju
Yoon, Ho Sup
Agarwal, Kan
format Conference or Workshop Item
author Jeon, Choon Ju
Yoon, Ho Sup
Agarwal, Kan
author_sort Jeon, Choon Ju
title The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II
title_short The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II
title_full The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II
title_fullStr The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II
title_full_unstemmed The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II
title_sort transcription factor tfiis zinc ribbon dipeptide asp-glu is critical for stimulation of elongation and rna cleavage by rna polymerase ii
publishDate 2012
url https://hdl.handle.net/10356/94050
http://hdl.handle.net/10220/7484
_version_ 1759854772321517568