Evidence map›Paper›PMID 37696373›Full record

ArticleInternational journal of biological macromolecules2023

Structural basis for evolutionarily conserved interactions between TFIIS and Paf1C.

Jie Gao, Miki Jishage, Yuzhu Wang, Rui Wang, Meng Chen, Zhongliang Zhu, Jiahai Zhang, Yating Diwu, Chao Xu, Shanhui Liao and 2 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of biological macromolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 77% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 2 countries.

Jie GaoMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China; Department of Ophthalmology, The Second Affiliated Hospital of Anhui Medical University, 678 Furong Road, Hefei, Anhui, PR China.
Miki JishageLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10065, USA.
Yuzhu WangMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China.
Rui WangMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China; Department of Anthropotomy and Histoembryology, Medical College, Henan University of Science and Technology, Luoyang, Henan 471023, PR China.
Meng ChenMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China.
Zhongliang ZhuMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China.
Jiahai ZhangMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China.
Yating DiwuMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China.
Chao XuMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China.
Shanhui LiaoMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China. Electronic address: ajsod@mail.ustc.edu.cn.
Robert G RoederLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10065, USA. Electronic address: roeder@mail.rockefeller.edu.
Xiaoming TuMOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Research Center for Interdisciplinary Sciences at the Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230022, PR China. Electronic address: xmtu@ustc.edu.cn.
University of Science and Technology of China · CNHefei National Center for Physical Sciences at Nanoscale · CNRockefeller University · USAnhui Medical University · CNHenan University of Science and Technology · CN

Funding

Mechanistic studies of transcription initiation and elongation functions of an RNA polymerase II variant, Pol II(G), that is implicated in development and cancerR01CA273709 · NCI · ROCKEFELLER UNIVERSITY · PI ROBERT G ROEDER · 2022 to 2026
$1.9M
NCI NIH HHS R01 CA273709
6 · The paper itself

Abstract

The elongation factor TFIIS interacts with Paf1C complex to facilitate processive transcription by Pol II. We here determined the crystal structure of the trypanosoma TFIIS LW domain in a complex with the LFG motif of Leo1, as well as the structures of apo-form TFIIS LW domains from trypanosoma, yeast and human. We revealed that all three TFIIS LW domains possess a conserved hydrophobic core that mediates their interactions with Leo1. Intriguingly, the structural study revealed that trypanosoma Leo1 binding induces the TFIIS LW domain to undergo a conformational change reflected in the length and orientation of α6 helix that is absent in the yeast and human counterparts. These differences explain the higher binding affinity of the TFIIS LW domain interacting with Leo1 in trypanosoma than in yeast and human, and indicate species-specific variations in the interactions. Importantly, the interactions between the TFIIS LW domain and an LFG motif of Leo1 were found to be critical for TFIIS to anchor the entire Paf1C complex. Thus, in addition to revealing a detailed structural basis for the TFIIS-Paf1C interaction, our studies also shed light on the origin and evolution of the roles of TFIIS and Paf1C complex in regulation of transcription elongation.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHumansRNA-Binding ProteinsRNA Polymerase IITranscriptional Elongation FactorsTranscription, GeneticLeo1 protein, S cerevisiaeRNA-Binding ProteinsRNA Polymerase IISaccharomyces cerevisiae ProteinsTranscriptional Elongation Factorstranscription factor S-IILeo1LW domainPaf1C complexProtein structureTFIISTranscription regulation

Identifiers

PMID37696373
PMCPMC11164251
OpenAlexW4386575443

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.