Evidence map›Paper›PMID 29661922›Full record

ArticleMolecular and cellular biology2018

Gpn2 and Rba50 Directly Participate in the Assembly of the Rpb3 Subcomplex in the Biogenesis of RNA Polymerase II.

Fanli Zeng, Yu Hua, Xiaoqin Liu, Sijie Liu, Kejing Lao, Ze Zhang, Daochun Kong

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 29 citations in OpenAlex.

  1. Dissection ofmBio · 2026
    Article
  2. Structure of cytoplasmic RNA polymerase II.Nature communications · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
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

7 authors at 3 institutions in 1 country.

Fanli Zeng *Peking-Tsinghua Center for Life Sciences, The National Laboratory of Protein and Plant Gene Research, The College of Life Sciences, Peking University, Beijing, China fanli.zeng@pku.edu.cn kongdc@pku.edu.cn.
Yu Hua *Peking-Tsinghua Center for Life Sciences, The National Laboratory of Protein and Plant Gene Research, The College of Life Sciences, Peking University, Beijing, China.
Xiaoqin LiuPeking-Tsinghua Center for Life Sciences, The National Laboratory of Protein and Plant Gene Research, The College of Life Sciences, Peking University, Beijing, China.
Sijie LiuPeking-Tsinghua Center for Life Sciences, The National Laboratory of Protein and Plant Gene Research, The College of Life Sciences, Peking University, Beijing, China.
Kejing LaoPeking-Tsinghua Center for Life Sciences, The National Laboratory of Protein and Plant Gene Research, The College of Life Sciences, Peking University, Beijing, China.
Ze ZhangCollege of Life Sciences, Hebei Agricultural University, Baoding, Hebei, China.
Daochun KongPeking-Tsinghua Center for Life Sciences, The National Laboratory of Protein and Plant Gene Research, The College of Life Sciences, Peking University, Beijing, China fanli.zeng@pku.edu.cn kongdc@pku.edu.cn.
Center for Life Sciences · CNHebei Agricultural University · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA polymerase II (RNAPII) is one of the central enzymes in cell growth and organizational development. It is a large macromolecular complex consisting of 12 subunits. Relative to the clear definition of RNAPII structure and biological function, the molecular mechanism of how RNAPII is assembled is poorly understood, and thus the key assembly factors acting for the assembly of RNAPII remain elusive. In this study, we identified two factors, Gpn2 and Rba50, that directly participate in the assembly of RNAPII. Gpn2 and Rba50 were demonstrated to interact with Rpb12 and Rpb3, respectively. An interaction between Gpn2 and Rba50 was also demonstrated. When Gpn2 and Rba50 are functionally defective, the assembly of the Rpb3 subcomplex is disrupted, leading to defects in the assembly of RNAPII. Based on these results, we conclude that Gpn2 and Rba50 directly participate in the assembly of the Rpb3 subcomplex and subsequently the biogenesis of RNAPII.

Indexed as

Amino Acid SequenceConserved SequenceGTP PhosphohydrolasesHumansModels, BiologicalMonomeric GTP-Binding ProteinsMultiprotein ComplexesMutationProtein MultimerizationProtein SubunitsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence Homology, Amino AcidGPN2 protein, S cerevisiaeGTP PhosphohydrolasesMonomeric GTP-Binding ProteinsMultiprotein ComplexesPOLR2C protein, humanProtein SubunitsRNA Polymerase IIRPB3 protein, S cerevisiaerpb3 protein, S pombeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteinsassembly factorGpn2Rba50RNA polymerase II

Identifiers

PMID29661922
PMCPMC6002695
OpenAlexW2800120922

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.