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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Artsimovitch, Irina Sevostyanova, Anastasia Deaconescu, Alexandra M. Grigorieff, Nikolaus |
| Description | Author Affiliation: Deaconescu AM ( Howard Hughes Medical Institute, The Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454, USA.); |
| Abstract | Transcription-coupled DNA repair targets DNA lesions that block progression of elongating RNA polymerases. In bacteria, the transcription-repair coupling factor (TRCF; also known as Mfd) SF2 ATPase recognizes RNA polymerase stalled at a site of DNA damage, removes the enzyme from the DNA, and recruits the Uvr(A)BC nucleotide excision repair machinery via UvrA binding. Previous studies of TRCF revealed a molecular architecture incompatible with UvrA binding, leaving its recruitment mechanism unclear. Here, we examine the UvrA recognition determinants of TRCF using X-ray crystallography of a core TRCF–UvrA complex and probe the conformational flexibility of TRCF in the absence and presence of nucleotides using small-angle X-ray scattering. We demonstrate that the C-terminal domain of TRCF is inhibitory for UvrA binding, but not RNA polymerase release, and show that nucleotide binding induces concerted multidomain motions. Our studies suggest that autoinhibition of UvrA binding in TRCF may be relieved only upon engaging the DNA damage. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 109 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2012-02-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphatases Metabolism Bacterial Proteins Physiology DNA Repair DNA-Binding Proteins Escherichia Coli Proteins Transcription Factors Antagonists & Inhibitors Chemistry Adenosine Triphosphate Amino Acid Sequence Crystallography, X-Ray DNA Damage DNA Helicases DNA, Bacterial Escherichia Coli Enzymology Genetics Hydrolysis Models, Molecular Molecular Sequence Data Protein Binding Protein Conformation Protein Interaction Mapping Protein Structure, Tertiary RNA Polymerase I Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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