当前位置: X-MOL 学术Proc. Natl. Acad. Sci. U.S.A. › 论文详情
Structural basis for CDK7 activation by MAT1 and Cyclin H [Biochemistry]
Proceedings of the National Academy of Sciences of the United States of America ( IF 9.412 ) Pub Date : 2020-10-14 , DOI: 10.1073/pnas.2010885117
Stefan Peissert, Andreas Schlosser, Rafaela Kendel, Jochen Kuper, Caroline Kisker

Cyclin-dependent kinase 7 (CDK7), Cyclin H, and the RING-finger protein MAT1 form the heterotrimeric CDK-activating kinase (CAK) complex which is vital for transcription and cell-cycle control. When associated with the general transcription factor II H (TFIIH) it activates RNA polymerase II by hyperphosphorylation of its C-terminal domain (CTD). In the absence of TFIIH the trimeric complex phosphorylates the T-loop of CDKs that control cell-cycle progression. CAK holds a special position among the CDK branch due to this dual activity and the dependence on two proteins for activation. We solved the structure of the CAK complex from the model organism Chaetomium thermophilum at 2.6-Å resolution. Our structure reveals an intricate network of interactions between CDK7 and its two binding partners MAT1 and Cyclin H, providing a structural basis for the mechanism of CDK7 activation and CAK activity regulation. In vitro activity measurements and functional mutagenesis show that CDK7 activation can occur independent of T-loop phosphorylation and is thus exclusively MAT1-dependent by positioning the CDK7 T-loop in its active conformation.

更新日期:2020-10-16

 

全部期刊列表>>
Springer 纳米技术权威期刊征稿
全球视野覆盖
施普林格·自然新
chemistry
3分钟学术视频演讲大赛
物理学研究前沿热点精选期刊推荐
自然职位线上招聘会
欢迎报名注册2020量子在线大会
化学领域亟待解决的问题
材料学研究精选新
GIANT
ACS ES&T Engineering
ACS ES&T Water
屿渡论文,编辑服务
ACS Publications填问卷
阿拉丁试剂right
西北大学
大连理工大学
湖南大学
华东师范大学
王要兵
浙江大学
隐藏1h前已浏览文章
课题组网站
新版X-MOL期刊搜索和高级搜索功能介绍
ACS材料视界
天合科研
x-mol收录
陆军军医大学
李霄鹏
廖矿标
试剂库存
down
wechat
bug