mirage

Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

DSpace/Manakin Repository

 

Search DR-NTU


Advanced Search Subject Search

Browse

My Account

Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

Show full item record

Title: Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS
Author: Qian, Xiuqu; Jeon, Choon Ju; Yoon, Ho Sup; Agarwal, Kan; Weiss, Michael A.
Copyright year: 1993
Abstract: Transcriptional elongation involves dynamic interactions among RNA polymerase and single-stranded and double stranded nucleic acids in the ternary complex1–4. In prokaryotes its regulation pro-vides an important mechanism of genetic control1. Analogous eukaryotic mechanisms are not well understood5, but may control expression of proto-oncogenes6,7 and viruses, including the human immunodeficiency virus HIV-1 (ref. 8). The highly conserved euk-aryotic transcriptional elongation factor TFIIS9 enables RNA polymerase II (RNAPII) to read though pause or termination sites, nucleosomes and sequence-specific DNA-binding proteins10–14. Two distinct domains of human TFIIS, which bind RNAPII and nucleic acids, regulate read-through10 and possibly nascent transcript cleavage11–15. Here we describe the three-dimensional NMR16 structure of a Cys4 nucleic-acid-binding domain from human TFIIS9,10. Unlike previously characterized zinc modules17–21, which contain an α-helix, this structure consists of a three-stranded β-sheet. Analogous Cys4 structural motifs may occur in other proteins involved in DNA or RNA trans-actions22–24, including RNAPII itself25. This new structure, desig-nated the Zn ribbon, extends the repertoire of Zn-mediated peptide architectures26 and highlights the growing recognition of the β-sheet as a motif of nucleic-acid recognition27,28.
Subject: DRNTU::Science::Biological sciences.
Type: Journal Article
Series/ Journal Title: Nature
School: School of Biological Sciences
Rights: © 1993 Nature Publishing Group. This is the author created version of a work that has been peer reviewed and accepted for publication by Nature, Nature Publishing Group. 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/10.1038/365277a0
Version: Accepted version

Files in this item

Files Size Format View
48. Structure o ... acid binding motif in.pdf 333.6Kb PDF View/Open
   

DOI Query

- Get published version (via Digital Object Identifier)
   

This item appears in the following Collection(s)

Show full item record

Statistics

Total views

All Items Views
Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS 362

Total downloads

All Bitstreams Views
48. Structure of a new nucleic acid binding motif in.pdf 144

Top country downloads

Country Code Views
United States of America 61
Singapore 23
China 14
India 7
Turkey 6

Top city downloads

city Views
Mountain View 46
Singapore 23
Ankara 4
Mumbai 4
Redwood City 4

Downloads / month

  2014-05 2014-06 2014-07 total
48. Structure of a new nucleic acid binding motif in.pdf 0 0 6 6