Open AccessStructure of TFIIK for phosphorylation of CTD of RNA polymerase II
Author(s) -
Trevor van Eeuwen,
Tao Li,
Hee Jong Kim,
Jose J. Gorbea Colón,
Mitchell I. Parker,
Roland L. Dunbrack,
Benjamin A. Garcia,
KuangLei Tsai,
Kenji Murakami
Publication year - 2021
Publication title -
science advances
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.928
H-Index - 146
ISSN - 2375-2548
DOI - 10.1126/sciadv.abd4420
Subject(s) - ctd , rna polymerase ii , polymerase , phosphorylation , transcription preinitiation complex , transcription factor ii f , transcription factor ii e , microbiology and biotechnology , transcription factor ii d , computational biology , chemistry , biology , genetics , rna dependent rna polymerase , gene , promoter , gene expression , geology , oceanography
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.