Insights into anti-termination regulation of the hut operon in Bacillus subtilis: importance of the dual RNA-binding surfaces of HutP
| Autor: | Penmetcha K. R. Kumar, Thirumananseri Kumarevel, Dhakshnamoorthy Balasundaresan, Subash C. B. Gopinath, Hiroshi Mizuno, Tomoko Misono |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Operon Molecular Sequence Data RNA-binding protein HutP Bacterial Proteins Transcription (biology) Gene expression Genetics Histidine RNA Messenger Binding site Terminator Regions Genetic Binding Sites Base Sequence biology RNA-Binding Proteins RNA Gene Expression Regulation Bacterial Molecular biology Cell biology Mutation biology.protein Nucleic Acid Conformation Terminator (franchise) Bacillus subtilis |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gkn199 |
| Popis: | The anti-termination protein, HutP, regulates the gene expression of the hut (histidine utilization) operon of Bacillus subtilis, by destabilizing the hut terminator RNA located upstream of the coding region encoding l-histidine degradation enzymes. On the basis of biochemical, in vivo and X-ray structural analyses, we now report that HutP uses its dual RNA-binding surfaces to access two XAG-rich regions (sites I and II) within the terminator RNA to mediate the destabilization process. In this process, HutP initiates destabilization at the 5′-end of its mRNA by binding to the first XAG-rich region (site I) and then accesses the second XAG-rich region (site II), located downstream of the stable G-C-rich segment of the terminator stem. By this action, HutP appears to disrupt the G-C-rich terminator stem, and thus prevents premature termination of transcription in the RNA segment preceding the regions encoding for the histidine degradation enzymes. |
| Databáze: | OpenAIRE |
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