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Phosphorylation of C-terminal domain of RNA polymerase II is not required in basal transcription

Hiroaki Serizawa
Joan Weliky Conaway
Ronald C. Conaway
Research27 May 1993
Nature

Volume: 363, P: 371-374
Association of Cdk-activating kinase subunits with transcription factor TFIIH

Hiroaki Serizawa
Tomi P. Mäkelä
Richard A. Young
Research16 Mar 1995
Nature

Volume: 374, P: 280-282
Orchestrating transcription with the pol II CTD

Ronald and Joan Conaway highlight studies that established the role of phosphorylation of the RNA polymerase II carboxy-terminal domain (CTD) in the transition from transcription initiation to elongation, which paved the ground for following work on the CTD in regulating co-transcriptional processes.

Ronald C. Conaway
Joan W. Conaway
Research Highlights18 Feb 2015
Nature Reviews Molecular Cell Biology

Volume: 16, P: 128
The hunt for RNA polymerase II elongation factors: a historical perspective

This personal Perspective by Joan and Ron Conaway describes the biochemical identification and characterization of three key transcription elongation factors, TFIIS, Elongin and ELL, and summarizes how the delineation of their functions has informed the understanding of the regulatory mechanisms that control elongation by RNA polymerase II.

Ronald C. Conaway
Joan W. Conaway
Reviews22 Aug 2019
Nature Structural & Molecular Biology

Volume: 26, P: 771-776
YY1 functions with INO80 to activate transcription

Yong Cai
Jingji Jin
Joan W Conaway
Research26 Aug 2007
Nature Structural & Molecular Biology

Volume: 14, P: 872-874
The 3′ Pol II pausing at replication-dependent histone genes is regulated by Mediator through Cajal bodies’ association with histone locus bodies

Transcription termination is generally accompanied by the 3′-end processing of transcripts. Here the authors demonstrate a role for Mediator in transcript end site proximal pausing of replication-dependent histone genes.

Hidefumi Suzuki
Ryota Abe
Hidehisa Takahashi
ResearchOpen Access25 May 2022
Nature Communications

Volume: 13, P: 1-24
TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin

Many proteins are assembled into damaged chromatins to repair DNA double-strand breaks (DSBs). Here, the authors show that TRIM29 binds to modified histone H3 and H4 tails following DSB formation and functions as a scaffold protein to assemble DNA repair proteins into chromatin.

Yasushi Masuda
Hidehisa Takahashi
Shigetsugu Hatakeyama
Research22 Jun 2015
Nature Communications

Volume: 6, P: 1-13
The role of Mediator and Little Elongation Complex in transcription termination

Mediator subunit MED26 was shown to help recruit Super Elongation Complex (SEC) or Little Elongation Complex (LEC) to control the expression of certain genes. Here, the authors provide evidence that MED26 recruits LEC to regulate transcription termination of non-polyadenylated genes, including snRNA and replication-dependent histone (RDH) genes at Cajal bodies.

Hidehisa Takahashi
Amol Ranjan
Shigetsugu Hatakeyama
ResearchOpen Access26 Feb 2020
Nature Communications

Volume: 11, P: 1-20
MED26 regulates the transcription of snRNA genes through the recruitment of little elongation complex

The little elongation complex (LEC) has been implicated in the regulation of Pol II-transcribed snRNA genes. Here, the authors show that MED26 recruits the LEC to a subset of Pol II-transcribed snRNAgenes through its N terminus, entailing a TAF7 to LEC switch that facilitates the transition from initiation to elongation.

Hidehisa Takahashi
Ichigaku Takigawa
Shigetsugu Hatakeyama
Research09 Jan 2015
Nature Communications

Volume: 6, P: 1-15
Mediator structure and rearrangements required for holoenzyme formation

Cryo-electron microscopy maps of the fission yeast Mediator complex and of a Mediator–RNA polymerase II holoenzyme reveal how changes in the Med14 subunit enable large-scale rearrangements of the Mediator structure that are essential for holoenzyme formation.

Kuang-Lei Tsai
Xiaodi Yu
Francisco J. Asturias
Research01 Mar 2017
Nature

Volume: 544, P: 196-201
CTD-dependent and -independent mechanisms govern co-transcriptional capping of Pol II transcripts

The co-transcriptional capping of transcripts synthesized by RNA Pol II is substantially more efficient than capping of free RNA, a process that has been shown to depend on CTD phosphorylation. Here the authors demonstrate that a CTD-independent mechanism functions in parallel with CTD-dependent processes to ensure efficient capping.

Melvin Noe Gonzalez
Shigeo Sato
Ronald C. Conaway
ResearchOpen Access23 Aug 2018
Nature Communications

Volume: 9, P: 1-13
Structure of the Cul1–Rbx1–Skp1–F box^Skp2 SCF ubiquitin ligase complex

Ning Zheng
Brenda A. Schulman
Nikola P. Pavletich
Research18 Apr 2002
Nature

Volume: 416, P: 703-709
A conserved Mediator–CDK8 kinase module association regulates Mediator–RNA polymerase II interaction

The CDK8 kinase module (CKM) is a subcomplex that interacts with Mediator and represses transcription. Structural and biochemical analyses now show that interaction of the CKM with Mediator interferes with C-terminal domain–dependent binding of RNA polymerase II to a previously unknown Mediator binding site and with holoenzyme formation, which forms the basis for CKM's repressive effect on transcription.

Kuang-Lei Tsai
Shigeo Sato
Francisco J Asturias
Research07 Apr 2013
Nature Structural & Molecular Biology

Volume: 20, P: 611-619
Genome-wide analysis of cis-regulatory changes underlying metabolic adaptation of cavefish

Genome-wide epigenomic profiling of liver tissue from one surface and two independent cave populations of Astyanax mexicanus sheds light on regulatory changes underlying metabolic adaptations to the nutrient-deprived cave environment.

Jaya Krishnan
Chris W. Seidel
Nicolas Rohner
Research12 May 2022
Nature Genetics

Volume: 54, P: 684-693

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Phosphorylation of C-terminal domain of RNA polymerase II is not required in basal transcription

Association of Cdk-activating kinase subunits with transcription factor TFIIH

Orchestrating transcription with the pol II CTD

The hunt for RNA polymerase II elongation factors: a historical perspective

YY1 functions with INO80 to activate transcription

The 3′ Pol II pausing at replication-dependent histone genes is regulated by Mediator through Cajal bodies’ association with histone locus bodies

TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin

The role of Mediator and Little Elongation Complex in transcription termination

MED26 regulates the transcription of snRNA genes through the recruitment of little elongation complex

Mediator structure and rearrangements required for holoenzyme formation

CTD-dependent and -independent mechanisms govern co-transcriptional capping of Pol II transcripts

Structure of the Cul1–Rbx1–Skp1–F box^Skp2 SCF ubiquitin ligase complex

A conserved Mediator–CDK8 kinase module association regulates Mediator–RNA polymerase II interaction

Genome-wide analysis of cis-regulatory changes underlying metabolic adaptation of cavefish

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