| | |  | | | | Record from Web of Science® | | | | | | |
| A new class of bacterial RNA polymerase inhibitor affects nucleotide addition |
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| Author(s): Artsimovitch I, Chu C, Lynch AS, Landick R |
| Source: SCIENCE Volume: 302 Issue: 5645 Pages: 650-654 Published: OCT 24 2003 |
| Times Cited: 33 References: 27 |
| Abstract: RNA polymerase (RNAP) is the central enzyme of gene expression. Despite availability of crystal structures, details of its nucleotide addition cycle remain obscure. We describe bacterial RNAP inhibitors (the CBR703 series) whose properties illuminate this mechanism. These compounds inhibit known catalytic activities of RNAP (nucleotide addition, pyrophosphorolysis, and Gre-stimulated transcript cleavage) but not translocation of RNA or DNA when translocation is uncoupled from catalysis. CBR703-resistance substitutions occur on an outside surface of RNAP opposite its internal active site. We propose that CBR703 compounds inhibit nucleotide addition allosterically by hindering movements of active site structures that are linked to the CBR703 binding site through a bridge helix. |
| Document Type: Article |
| Language: English |
| Reprint Address: Lynch, AS (reprint author), Cumbre Inc, 1502 Viceroy Dr, Dallas, TX 75235 USA |
Addresses:
1. Cumbre Inc, Dallas, TX 75235 USA
2. Univ Wisconsin, Dept Bacteriol, Madison, WI 53706 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: 735MV |
| ISSN: 0036-8075 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |