Structure of the human Mediator-bound transcription preinitiation complex

Author:

Abdella R.12ORCID,Talyzina A.12ORCID,Chen S.12ORCID,Inouye C. J.3456ORCID,Tjian R.3456ORCID,He Y.1278ORCID

Affiliation:

1. Department of Molecular Biosciences, Northwestern University, Evanston, IL, USA.

2. Interdisciplinary Biological Sciences Program, Northwestern University, Evanston, IL, USA.

3. Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA.

4. Li Ka Shing Center for Biomedical and Health Sciences, University of California, Berkeley, Berkeley, CA, USA.

5. CIRM Center of Excellence, University of California, Berkeley, Berkeley, CA, USA.

6. Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA, USA.

7. Chemistry of Life Processes Institute, Northwestern University, Evanston, IL, USA.

8. Robert H. Lurie Comprehensive Cancer Center of Northwestern University, Northwestern University, Chicago, IL, USA.

Abstract

Mediating transcription The Mediator complex is recruited by transcription factors to all protein-coding genes in eukaryotes and helps to assemble the machinery necessary to transcribe the gene. Abdella et al. present the cryo–electron microscopy structure of the human Mediator-bound preinitiation complex (Med-PIC). The structure shows how Mediator positions the long, flexible C-terminal domain of RNA polymerase II to be phosphorylated by the kinase CDK7, a crucial step for further processing of the RNA into a mature RNA. Most sites where transcription factors bind to Mediator are flexibly tethered to the complex, allowing the large Med-PIC to assemble at any gene. Science , this issue p. 52

Funder

National Institutes of Health

Howard Hughes Medical Institute

American Cancer Society

National Cancer Institute

National Institute of General Medical Sciences

Oregon Health and Science University

He He

Chicago Biomedical Consortium

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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