Evidence map›Paper›PMID 23303773›Full record

ArticleNucleic acids research2013

Transcription-independent role for human mitochondrial RNA polymerase in mitochondrial ribosome biogenesis.

Yulia V Surovtseva, Gerald S Shadel

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. The role of m5C, m1A and m7G modifications in tumors of urinary system.Frontiers in cell and developmental biology · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Mitochondrial protein interactome elucidated by chemical cross-linking mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Mitochondrial transcription in mammalian cells.Frontiers in bioscience (Landmark edition) · 2017
    Review
  11. Mitochondrial BMI1 maintains bioenergetic homeostasis in cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
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  20. 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

2 authors at 1 institution in 1 country.

Yulia V SurovtsevaDepartment of Pathology, Yale University School of Medicine, New Haven, CT 06520, USA.
Gerald S Shadel
Yale University · US

Funding

Nuclear Control of Mitochondrial Gene ExpressionR01HL059655 · NHLBI · YALE UNIVERSITY · PI SHADEL, GERALD · 1997 to 2011
$3.1M
Analysis of Mammalian Mitochondrial Transcription MachineryF32GM093590 · NIGMS · YALE UNIVERSITY · PI SUROVTSEVA, YULIA · 2010 to 2011
$93k
NHLBI NIH HHS R01 HL-059655NIGMS NIH HHS F32 GM-093590
6 · The paper itself

Abstract

Human mitochondrial RNA polymerase, POLRMT, is required for mitochondrial DNA (mtDNA) transcription and forms initiation complexes with human mitochondrial transcription factor B2 (h-mtTFB2). However, POLRMT also interacts with the paralogue of h-mtTFB2, h-mtTFB1, which is a 12S ribosomal RNA methyltransferase required for small (28S) mitochondrial ribosome subunit assembly. Herein, we show that POLRMT associates with h-mtTFB1 in 28S mitochondrial ribosome complexes that are stable in the absence of mitochondrial transcription and distinct from transcription complexes containing POLRMT and h-mtTFB2. Overexpression of POLRMT in HeLa cells increases 12S rRNA methylation by h-mtTFB1 and reduces the steady-state levels of mtDNA-encoded proteins and respiration, apparently because of a decrease in fully assembled 55S mitochondrial ribosomes. We propose that POLRMT interacts directly with h-mtTFB1 in 28S mitochondrial ribosomes to augment its 12S rRNA methyltransferase activity, and that together they provide a checkpoint for proper 28S and 55S mitochondrial ribosome assembly. Thus, POLRMT is multi-functional, forming distinct protein complexes that regulate different steps in mitochondrial gene expression, at least one of which does not involve transcription per se. The significance of these results is discussed with regard to the mechanism and regulation of human mitochondrial gene expression and the potential multi-functionality of RNA polymerases in general.

Indexed as

Cell RespirationDNA-Binding ProteinsDNA-Directed RNA PolymerasesHeLa CellsHumansMethyltransferasesMitochondriaMitochondrial ProteinsRibosomesRNA, RibosomalTranscription FactorsTranscription, GeneticDNA-Binding ProteinsDNA-Directed RNA PolymerasesMethyltransferasesMitochondrial ProteinsPOLRMT protein, humanRNA, RibosomalRNA, ribosomal, 12STFB1M protein, humanTFB2M protein, humanTranscription Factors

Identifiers

PMID23303773
PMCPMC3575816
OpenAlexW2008247125

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.