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Structure and dynamics of the RNAPII CTDsome with Rtt103
O. Jasnovidova, T. Klumpler, K. Kubicek, S. Kalynych, P. Plevka, R. Stefl,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem, audiovizuální média
NLK
Free Medical Journals
od 1915 do Před 6 měsíci
Freely Accessible Science Journals
od 1915 do Před 6 měsíci
PubMed Central
od 1915 do Před 6 měsíci
Europe PubMed Central
od 1915 do Před 6 měsíci
Open Access Digital Library
od 1915-01-01
Open Access Digital Library
od 1915-01-15
PubMed
29073019
DOI
10.1073/pnas.1712450114
Knihovny.cz E-zdroje
- MeSH
- interakční proteinové domény a motivy MeSH
- krystalografie rentgenová MeSH
- magnetická rezonanční spektroskopie MeSH
- multimerizace proteinu MeSH
- RNA-polymerasa II metabolismus MeSH
- Saccharomyces cerevisiae - proteiny chemie metabolismus MeSH
- sekvence aminokyselin MeSH
- transkripční faktory chemie metabolismus MeSH
- Publikační typ
- audiovizuální média MeSH
- časopisecké články MeSH
- práce podpořená grantem MeSH
RNA polymerase II contains a long C-terminal domain (CTD) that regulates interactions at the site of transcription. The CTD architecture remains poorly understood due to its low sequence complexity, dynamic phosphorylation patterns, and structural variability. We used integrative structural biology to visualize the architecture of the CTD in complex with Rtt103, a 3'-end RNA-processing and transcription termination factor. Rtt103 forms homodimers via its long coiled-coil domain and associates densely on the repetitive sequence of the phosphorylated CTD via its N-terminal CTD-interacting domain. The CTD-Rtt103 association opens the compact random coil structure of the CTD, leading to a beads-on-a-string topology in which the long rod-shaped Rtt103 dimers define the topological and mobility restraints of the entire assembly. These findings underpin the importance of the structural plasticity of the CTD, which is templated by a particular set of CTD-binding proteins.
Citace poskytuje Crossref.org
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