Structural insights into the Cyclin T1–Tat–TAR RNA transcription activation complex from EIAV
| Autor: | Kanchan Anand, Klaus Scheffzek, Karin Vogel-Bachmayr, Antje Schulte, Matthias Geyer |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Cyclin T1 biology RNA RNA-dependent RNA polymerase RNA polymerase II RNA-binding protein Crystallography X-Ray Models Biological Molecular biology Long terminal repeat Structural Biology Cyclins Gene Products tat Cyclin-dependent kinase complex biology.protein Animals RNA Viral Horses Protein Structure Quaternary Molecular Biology Infectious Anemia Virus Equine Cyclin |
| Zdroj: | Nature Structural & Molecular Biology. 15:1287-1292 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsmb.1513 |
| Popis: | The replication of many retroviruses is mediated by a transcriptional activator protein, Tat, which activates RNA polymerase II at the level of transcription elongation. Tat interacts with Cyclin T1 of the positive transcription-elongation factor P-TEFb to recruit the transactivation-response TAR RNA, which acts as a promoter element in the transcribed 5' end of the viral long terminal repeat. Here we present the structure of the cyclin box domain of Cyclin T1 in complex with the Tat protein from the equine infectious anemia virus and its corresponding TAR RNA. The basic RNA-recognition motif of Tat adopts a helical structure whose flanking regions interact with a cyclin T-specific loop in the first cyclin box repeat. Together, both proteins coordinate the stem-loop structure of TAR. Our findings show that Tat binds to a surface on Cyclin T1 similar to where recognition motifs from substrate and inhibitor peptides were previously found to interact within Cdk-cyclin pairs. |
| Databáze: | OpenAIRE |
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