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Structure of TFIIK for phosphorylation of CTD of RNA polymerase II.

ABSTRACT: 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.

SUBMITTER: van Eeuwen T

PROVIDER: S-EPMC8026125 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Structure of TFIIK for phosphorylation of CTD of RNA polymerase II.

van Eeuwen Trevor T Li Tao T Kim Hee Jong HJ Gorbea Colón Jose J JJ Parker Mitchell I MI Dunbrack Roland L RL Garcia Benjamin A BA Tsai Kuang-Lei KL Murakami Kenji K

Science advances 20210407 15

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 MA ...[more]

PMID: 33827808

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