A novel RNA polymerase‐binding protein that interacts with a sigma‐factor docking site
| Autor: | Ann Hochschild, Caterina Alfano, Ewelina M. Krysztofinska, Rivka L. Isaacson, Cinthia P. Garcia, Anna F. Wang Erickson, Padraig Deighan, Kelsey Barrasso, Santiago Martínez-Lumbreras, Richard Losick, Arjun Thapaliya, Amy H. Camp, Shanshan Chen |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Transcription Genetic Anti-sigma factors Sigma Factor RNA polymerase II Microbiology Article 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Sigma factor RNA polymerase Journal Article RNA polymerase I Molecular Biology RNA polymerase II holoenzyme Spores Bacterial biology General transcription factor RNA-Binding Proteins DNA-Directed RNA Polymerases Gene Expression Regulation Bacterial Molecular biology Protein Structure Tertiary Cell biology 030104 developmental biology chemistry biology.protein Transcription factor II D Bacillus subtilis Protein Binding Transcription Factors |
| Zdroj: | Wang Erickson, A F, Deighan, P, Chen, S, Barrasso, K, Garcia, C P, Martínez-Lumbreras, S, Alfano, C, Krysztofinska, E M, Thapaliya, A, Camp, A H, Isaacson, R L, Hochschild, A & Losick, R 2017, ' A Novel RNA Polymerase-binding Protein that interacts with a Sigma-Factor Docking Site ', Molecular Microbiology . https://doi.org/10.1111/mmi.13724 |
| ISSN: | 1365-2958 0950-382X |
| Popis: | Sporulation in Bacillus subtilis is governed by a cascade of alternative RNA polymerase sigma factors. We previously identified a small protein Fin that is produced under the control of the sporulation sigma factor σ(F) to create a negative feedback loop that inhibits σ(F) -directed gene transcription. Cells deleted for fin are defective for spore formation and exhibit increased levels of σ(F) -directed gene transcription. Based on pull-down experiments, chemical crosslinking, bacterial two-hybrid experiments, and nuclear magnetic resonance chemical shift analysis, we now report that Fin binds to RNA polymerase and specifically to the coiled-coil region of the β' subunit. The coiled-coil is a docking site for sigma factors on RNA polymerase, and evidence is presented that the binding of Fin and σ(F) to RNA polymerase is mutually exclusive. We propose that Fin functions by a mechanism distinct from that of classic sigma factor antagonists (anti-σ factors), which bind directly to a target sigma factor to prevent its association with RNA polymerase, and instead functions to inhibit σ(F) by competing for binding to the β' coiled-coil. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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