Evidence map›Paper›PMID 12697831›Full record

ArticleMolecular and cellular biology2003

Loss of the Rpb4/Rpb7 subcomplex in a mutant form of the Rpb6 subunit shared by RNA polymerases I, II, and III.

Qian Tan, Meredith H Prysak, Nancy A Woychik

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  3. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
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  5. Article
  6. Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021
    Review
  7. Article
  8. Article
  9. Distinct pathways of RNA polymerase regulation by a phage-encoded factor.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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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

3 authors at 1 institution in 1 country.

Qian TanDepartment of Molecular Genetics, Microbiology and Immunology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854-5635, USA.
Meredith H Prysak
Nancy A Woychik
Rutgers, The State University of New Jersey · US

Funding

VIRUS-HOST INTERACTIONS IN EUKARYOTIC CELLST32AI007403 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI BREWER, GARY A. · 1991 to 2014
$1.7M
DISSECTION OF YEAST RNA POLYMERASE II FUNCTIONR01GM055736 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI WOYCHIK, NANCY ANN · 1997 to 2001
$504k
NIAID NIH HHS 2 T32 AI07403-10NIAID NIH HHS T32 AI007403NIGMS NIH HHS GM 55736
6 · The paper itself

Abstract

We have identified a conditional mutation in the shared Rpb6 subunit, assembled in RNA polymerases I, II, and III, that illuminated a new role that is independent of its assembly function. RNA polymerase II and III activities were significantly reduced in mutant cells before and after the shift to nonpermissive temperature. In contrast, RNA polymerase I was marginally affected. Although the Rpb6 mutant strain contained two mutations (P75S and Q100R), the majority of growth and transcription defects originated from substitution of an amino acid nearly identical in all eukaryotic counterparts as well as bacterial omega subunits (Q100R). Purification of mutant RNA polymerase II revealed that two subunits, Rpb4 and Rpb7, are selectively lost in mutant cells. Rpb4 and Rpb7 are present at substoichiometric levels, form a dissociable subcomplex, are required for RNA polymerase II activity at high temperatures, and have been implicated in the regulation of enzyme activity. Interaction experiments support a direct association between the Rpb6 and Rpb4 subunits, indicating that Rpb6 is one point of contact between the Rpb4/Rpb7 subcomplex and RNA polymerase II. The association of Rpb4/Rpb7 with Rpb6 suggests that analogous subunits of each RNA polymerase impart class-specific functions through a conserved core subunit.

Indexed as

MutationAmino Acid SequenceConserved SequenceDNA-Directed RNA PolymerasesFungal ProteinsMacromolecular SubstancesModels, MolecularMolecular Sequence DataProtein ConformationProtein SubunitsRNA, MessengerRNA Polymerase IRNA Polymerase IIRNA Polymerase IIISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Directed RNA PolymerasesFungal ProteinsMacromolecular SubstancesProtein SubunitsRNA, MessengerRNA Polymerase IRNA Polymerase IIRNA Polymerase IIIRPB4 protein, S cerevisiaeRPB7 protein, S cerevisiaeRPO26 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID12697831
PMCPMC153193
OpenAlexW2059768092

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.