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Journal article
Structure of TFIIK for phosphorylation of CTD of RNA polymerase II
Science advances, v 7(15)
09 Apr 2021
PMID: 33827808
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Cryo-EM structure of TFIIK provides insight into CTD phosphorylation of RNA polymerase II in the preinitiation-Mediator complex.
During transcription initiation, the general transcription factor TFIIH marks RNA polymerase II by phosphorylating Ser5 of the carboxyl-terminal domain (CTD) of Rpb1, which is followed by extensive modifications coupled to transcription elongation, mRNA processing, and histone dynamics. We have determined a 3.5-Å resolution cryo–electron microscopy (cryo-EM) structure of the TFIIH kinase module (TFIIK in yeast), which is composed of Kin28, Ccl1, and Tfb3, yeast homologs of CDK7, cyclin H, and MAT1, respectively. The carboxyl-terminal region of Tfb3 was lying at the edge of catalytic cleft of Kin28, where a conserved Tfb3 helix served to stabilize the activation loop in its active conformation. By combining the structure of TFIIK with the previous cryo-EM structure of the preinitiation complex, we extend the previously proposed model of the CTD path to the active site of TFIIK.
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Details
- Title
- Structure of TFIIK for phosphorylation of CTD of RNA polymerase II
- Creators
- Trevor van Eeuwen - University of PennsylvaniaTao Li - The University of Texas Health Science Center at HoustonHee Jong Kim - University of PennsylvaniaJose J. Gorbea Colón - Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA., Biochemistry and Molecular Biophysics Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USAMitchell I. Parker - Fox Chase Cancer CenterRoland L. Dunbrack - Fox Chase Cancer CenterBenjamin A. Garcia - University of PennsylvaniaKuang-Lei Tsai - The University of Texas Health Science Center at HoustonKenji Murakami - University of PennsylvaniaXiaohua Hu - Information Science (Informatics)
- Publication Details
- Science advances, v 7(15)
- Publisher
- American Association for the Advancement of Science (AAAS)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Information Science; College of Medicine
- Web of Science ID
- WOS:000637819900004
- Scopus ID
- 2-s2.0-85103998713
- Other Identifier
- 991019201218104721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology