RNA Polymerase Accommodates a Pause RNA Hairpin by Global Conformational Rearrangements that Prolong Pausing
Autor: | Jin Young Kang, Michael J. Bellecourt, Seth A. Darst, Rachel A. Mooney, Tatiana V. Mishanina, Robert Landick |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Conformational change RNA Folding Transcription Genetic Operon Protein domain Biology Article 03 medical and health sciences chemistry.chemical_compound Allosteric Regulation Protein Domains Transcription (biology) RNA polymerase Gene expression Escherichia coli Molecular Biology Escherichia coli Proteins RNA Cell Biology DNA-Directed RNA Polymerases Cell biology enzymes and coenzymes (carbohydrates) RNA Bacterial 030104 developmental biology chemistry bacteria DNA |
Zdroj: | Molecular cell. 69(5) |
ISSN: | 1097-4164 |
Popis: | Sequence-specific pausing by RNA polymerase (RNAP) during transcription plays crucial and diverse roles in gene expression. In bacteria, RNA structures are thought to fold within the RNA exit channel of the RNAP and can increase pause lifetimes significantly. The biophysical mechanism of pausing is uncertain. We used single-particle cryo-EM to determine structures of paused complexes, including a 3.8-A structure of an RNA hairpin-stabilized, paused RNAP that coordinates RNA folding in the his operon attenuation control region of E. coli. The structures revealed a half-translocated pause state (RNA post-translocated, DNA pre-translocated) that can explain transcriptional pausing and a global conformational change of RNAP that allosterically inhibits trigger loop folding and can explain pause hairpin action. Pause hairpin interactions with the RNAP RNA exit channel suggest how RNAP guides the formation of nascent RNA structures. |
Databáze: | OpenAIRE |
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