RNA polymerase pausing and nascent-RNA structure formation are linked through clamp-domain movement
| Autor: | Tricia A. Windgassen, Pyae P Hein, Robert Landick, Rachel A. Mooney, Kellie E. Kolb, Seth A. Darst, Michael J. Bellecourt |
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| Rok vydání: | 2014 |
| Předmět: |
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Molecular RNA Folding RNA-induced transcriptional silencing Protein Conformation Molecular Sequence Data RNA-dependent RNA polymerase Biology 03 medical and health sciences chemistry.chemical_compound Structural Biology RNA polymerase Catalytic Domain RNA polymerase I Escherichia coli Amino Acid Sequence Molecular Biology 030304 developmental biology 0303 health sciences Base Sequence Escherichia coli Proteins 030302 biochemistry & molecular biology RNA DNA-Directed RNA Polymerases Non-coding RNA enzymes and coenzymes (carbohydrates) Biochemistry chemistry RNA editing Biophysics bacteria Nucleic Acid Conformation Small nuclear RNA |
| Zdroj: | Nature structuralmolecular biology. 21(9) |
| ISSN: | 1545-9985 |
| Popis: | The rates of RNA synthesis and the folding of nascent RNA into biologically active structures are linked via pausing by RNA polymerase (RNAP). Structures that form within the RNA-exit channel can either increase pausing by interacting with RNAP or decrease pausing by preventing backtracking. Conversely, pausing is required for proper folding of some RNAs. Opening of the RNAP clamp domain has been proposed to mediate some effects of nascent-RNA structures. However, the connections among RNA structure formation and RNAP clamp movement and catalytic activity remain uncertain. Here, we assayed exit-channel structure formation in Escherichia coli RNAP with disulfide cross-links that favor closed- or open-clamp conformations and found that clamp position directly influences RNA structure formation and RNAP catalytic activity. We report that exit-channel RNA structures slow pause escape by favoring clamp opening through interactions with the flap that slow translocation. |
| Databáze: | OpenAIRE |
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