K
Kuang-Lei Tsai
Researcher at University of Texas Health Science Center at Houston
Publications - 26
Citations - 1777
Kuang-Lei Tsai is an academic researcher from University of Texas Health Science Center at Houston. The author has contributed to research in topics: Mediator & RNA polymerase II. The author has an hindex of 14, co-authored 22 publications receiving 1398 citations. Previous affiliations of Kuang-Lei Tsai include University of Texas MD Anderson Cancer Center & Scripps Research Institute.
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Journal ArticleDOI
Structure of a designed protein cage that self-assembles into a highly porous cube.
Yen-Ting Lai,Eamonn Reading,Greg L. Hura,Kuang-Lei Tsai,Arthur Laganowsky,Francisco J. Asturias,John A. Tainer,Carol V. Robinson,Todd O. Yeates +8 more
TL;DR: These studies show that accurate design of large porous assemblies with specific shapes is feasible, while further specificity improvements will likely require limiting flexibility to select against alternative forms.
Journal ArticleDOI
A conserved Mediator–CDK8 kinase module association regulates Mediator–RNA polymerase II interaction
Kuang-Lei Tsai,Shigeo Sato,Chieri Tomomori-Sato,Ronald C. Conaway,Ronald C. Conaway,Joan W. Conaway,Joan W. Conaway,Francisco J. Asturias +7 more
TL;DR: The results reveal the basis for CKM repression, clarify the origin of the connection between CKM subunits and the CTD and suggest that a combination of competitive interactions and conformational changes that facilitate holoenzyme formation underlie the mechanism of transcription regulation by Mediator.
Journal ArticleDOI
Subunit Architecture and Functional Modular Rearrangements of the Transcriptional Mediator Complex
Kuang-Lei Tsai,Chieri Tomomori-Sato,Shigeo Sato,Ronald C. Conaway,Joan W. Conaway,Joan W. Conaway,Francisco J. Asturias +6 more
TL;DR: Conservation across eukaryotes of Mediator structure, subunit organization, and RNA polymerase II interaction suggest conservation of fundamental aspects of the Mediator mechanism.
Journal ArticleDOI
Crystal structure of the human FOXO3a-DBD/DNA complex suggests the effects of post-translational modification.
TL;DR: It is demonstrated that the methyl groups of specific thymine bases within the consensus sequence are important for FOXO3a-DBD recognition of the consensus binding site.
Journal ArticleDOI
Mediator structure and rearrangements required for holoenzyme formation
Kuang-Lei Tsai,Xiaodi Yu,Sneha Gopalan,Ti-Chun Chao,Ying Zhang,Laurence Florens,Michael P. Washburn,Michael P. Washburn,Kenji Murakami,Ronald C. Conaway,Ronald C. Conaway,Joan W. Conaway,Joan W. Conaway,Francisco J. Asturias +13 more
TL;DR: This study suggests that access to different conformations and crosstalk between structural elements are essential for the Mediator regulation mechanism, and could explain the capacity of the complex to integrate multiple regulatory signals.