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  Structure of Ctk3, a subunit of the RNA polymerase II CTD kinase complex, reveals a non-canonical CTD-interacting domain fold.

Mühlbacher, W., Mayer, A., Sun, M., Remmert, M., Cheung, A. C. M., Niesser, J., et al. (2015). Structure of Ctk3, a subunit of the RNA polymerase II CTD kinase complex, reveals a non-canonical CTD-interacting domain fold. Proteins: Structure, Function, and Bioinformatics, 83(10), 1849-1858. doi:10.1002/prot.24869.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-2ABB-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-10EB-0
Genre: Journal Article

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 Creators:
Mühlbacher, W., Author
Mayer, A., Author
Sun, M., Author
Remmert, M., Author
Cheung, A. C. M., Author
Niesser, J., Author
Söding, J.1, Author              
Cramer, P.2, Author              
Affiliations:
1Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              
2Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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Free keywords: Structural biology;X-ray crystallography;gene transcription;RNA polymerase II;C-terminal repeat domain (CTD);cyclin-dependent kinase
 Abstract: CTDK-I is a yeast kinase complex that phosphorylates the C-terminal repeat domain (CTD) of RNA polymerase II (Pol II) to promote transcription elongation. CTDK-I contains the cyclin-dependent kinase Ctk1 (homologous to human CDK9/CDK12), the cyclin Ctk2 (human cyclin K), and the yeast-specific subunit Ctk3, which is required for CTDK-I stability and activity. Here we predict that Ctk3 consists of a N-terminal CTD-interacting domain (CID) and a C-terminal three-helix bundle domain. We determine the X-ray crystal structure of the N-terminal domain of the Ctk3 homologue Lsg1 from the fission yeast Schizosaccharomyces pombe at 2.0 Å resolution. The structure reveals eight helices arranged into a right-handed superhelical fold that resembles the CID domain present in transcription termination factors Pcf11, Nrd1, and Rtt103. Ctk3 however shows different surface properties and no binding to CTD peptides. Together with the known structure of Ctk1 and Ctk2 homologues, our results lead to a molecular framework for analyzing the structure and function of the CTDK-I complex. This article is protected by copyright. All rights reserved.

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Language(s): eng - English
 Dates: 2015-07-282015-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/prot.24869
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Title: Proteins: Structure, Function, and Bioinformatics
Source Genre: Journal
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Pages: - Volume / Issue: 83 (10) Sequence Number: - Start / End Page: 1849 - 1858 Identifier: ISSN: 0887-3585