Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex

The C-terminal domain (CTD) kinase I (CTDK-1) complex is the primary RNA Polymerase II (Pol II) CTD Ser2 kinase in budding yeast. CTDK-1 consists of a cyclin-dependent kinase (CDK) Ctk1, a cyclin Ctk2, and a unique subunit Ctk3 required for CTDK-1 activity. Here, we present a crystal structure of CT...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2021-01, Vol.118 (3), p.1-7
Main Authors: Xie, Yihu, Lord, Christopher L., Clarke, Bradley P., Ivey, Austin L., Hill, Pate S., McDonald, W. Hayes, Wente, Susan R., Ren, Yi
Format: Article
Language:English
Subjects:
Biological Sciences
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Summary:The C-terminal domain (CTD) kinase I (CTDK-1) complex is the primary RNA Polymerase II (Pol II) CTD Ser2 kinase in budding yeast. CTDK-1 consists of a cyclin-dependent kinase (CDK) Ctk1, a cyclin Ctk2, and a unique subunit Ctk3 required for CTDK-1 activity. Here, we present a crystal structure of CTDK-1 at 1.85-Å resolution. The structure reveals that, compared to the canonical two-component CDK-cyclin system, the third component Ctk3 of CTDK-1 plays a critical role in Ctk1 activation by stabilizing a key element of CDK regulation, the T-loop, in an active conformation. In addition, Ctk3 contributes to the assembly of CTDK-1 through extensive interactions with both Ctk1 and Ctk2. We also demonstrate that CTDK-1 physically and genetically interacts with the serine/arginine-like protein Gbp2. Together, the data in our work reveal a regulatory mechanism of CDK complexes.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.2019163118