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DOI | 10.1073/pnas.2019163118 |
Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex | |
Xie Y.; Lord C.L.; Clarke B.P.; Ivey A.L.; Hill P.S.; Hayes McDonald W.; Wente S.R.; Ren Y. | |
发表日期 | 2021 |
ISSN | 00278424 |
卷号 | 118期号:3 |
英文摘要 | 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. © 2021 National Academy of Sciences. All rights reserved. |
英文关键词 | Cyclin-dependent kinase | X-ray crystallography | transcription | mRNA processing |
语种 | 英语 |
scopus关键词 | cyclin dependent kinase; cycline; fungal RNA; protein C terminal domain kinase 1; protein Ctk1; protein Ctk3; protein Gbp2; RNA polymerase II; serine arginine rich protein; unclassified drug; Article; crystal structure; enzyme activation; enzyme mechanism; enzyme regulation; nonhuman; priority journal; protein conformation; protein protein interaction; protein stability; protein structure |
来源期刊 | Proceedings of the National Academy of Sciences of the United States of America
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文献类型 | 期刊论文 |
条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/180945 |
作者单位 | Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, United States; Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, United States; Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, United States |
推荐引用方式 GB/T 7714 | Xie Y.,Lord C.L.,Clarke B.P.,et al. Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex[J],2021,118(3). |
APA | Xie Y..,Lord C.L..,Clarke B.P..,Ivey A.L..,Hill P.S..,...&Ren Y..(2021).Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex.Proceedings of the National Academy of Sciences of the United States of America,118(3). |
MLA | Xie Y.,et al."Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex".Proceedings of the National Academy of Sciences of the United States of America 118.3(2021). |
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