RNA polymerase and transcription elongation factor Spt4/5 complex structure
| Autor: | Daniel Bose, Zahirah M. Yusoff, Kevin J. Baker, Xiaodong Zhang, Katsuhiko S. Murakami, Brianna J. Klein |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Transcription Genetic Chromosomal Proteins Non-Histone DNA polymerase II Molecular Sequence Data RNA polymerase II DNA-Directed DNA Polymerase Crystallography X-Ray chemistry.chemical_compound RNA polymerase Nucleic Acids Animals Humans Amino Acid Sequence RNA polymerase II holoenzyme Polymerase Transcription bubble Multidisciplinary DNA clamp biology General transcription factor Sequence Homology Amino Acid Cryoelectron Microscopy Nuclear Proteins DNA DNA-Directed RNA Polymerases Biological Sciences Pyrococcus furiosus Biochemistry chemistry biology.protein Transcriptional Elongation Factors |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 108(2) |
| ISSN: | 1091-6490 |
| Popis: | Spt4/5 in archaea and eukaryote and its bacterial homolog NusG is the only elongation factor conserved in all three domains of life and plays many key roles in cotranscriptional regulation and in recruiting other factors to the elongating RNA polymerase. Here, we present the crystal structure of Spt4/5 as well as the structure of RNA polymerase-Spt4/5 complex using cryoelectron microscopy reconstruction and single particle analysis. The Spt4/5 binds in the middle of RNA polymerase claw and encloses the DNA, reminiscent of the DNA polymerase clamp and ring helicases. The transcription elongation complex model reveals that the Spt4/5 is an upstream DNA holder and contacts the nontemplate DNA in the transcription bubble. These structures reveal that the cellular RNA polymerases also use a strategy of encircling DNA to enhance its processivity as commonly observed for many nucleic acid processing enzymes including DNA polymerases and helicases. |
| Databáze: | OpenAIRE |
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