Structural basis of Q-dependent transcription antitermination
| العنوان: | Structural basis of Q-dependent transcription antitermination |
|---|---|
| المؤلفون: | Shenghai Chang, Tongguan Tian, Xiang Gao, Jing Shi, Bo Gao, Yu Feng, Linlin You, Zhaoyang Yu, Xing Zhang, Yu Zhang, Aijia Wen |
| المصدر: | Nature Communications Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019) |
| بيانات النشر: | Springer Science and Business Media LLC, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | 0301 basic medicine, Transcription, Genetic, Science, General Physics and Astronomy, 02 engineering and technology, Article, General Biochemistry, Genetics and Molecular Biology, Bacteriophage, Viral Proteins, 03 medical and health sciences, chemistry.chemical_compound, Transcription (biology), RNA polymerase, Escherichia coli, Bacteriophages, A-DNA, lcsh:Science, Promoter Regions, Genetic, Multidisciplinary, biology, Cryoelectron Microscopy, RNA, DNA-Directed RNA Polymerases, General Chemistry, 021001 nanoscience & nanotechnology, biology.organism_classification, Cell biology, enzymes and coenzymes (carbohydrates), Transcription antitermination, 030104 developmental biology, chemistry, Codon, Terminator, lcsh:Q, Structural biology, 0210 nano-technology, Transcription, Late gene, DNA |
| الوصف: | Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (QI and QII) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, QI forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well. Bacteriophage Q protein serves as a model regulator for the study of transcription elongation. Here the authors report a cryo-EM structure of an intact Q-engaged arrested complex, revealing the interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. |
| تدمد: | 2041-1723 |
| DOI: | 10.1038/s41467-019-10958-8 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03e9bbb3d33ad18c9250096e3ffd4dbb https://doi.org/10.1038/s41467-019-10958-8 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....03e9bbb3d33ad18c9250096e3ffd4dbb |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20411723 |
|---|---|
| DOI: | 10.1038/s41467-019-10958-8 |