Evidence map›Paper›PMID 17337445›Full record

ArticleThe Journal of biological chemistry2007

Human mitochondrial ribosomal protein MRPL12 interacts directly with mitochondrial RNA polymerase to modulate mitochondrial gene expression.

Zhibo Wang, Justin Cotney, Gerald S Shadel

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

60 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Human Mitochondrial RNA Processing and Modifications: Overview.International journal of molecular sciences · 2021
    Review
  8. ING2 Controls Mitochondrial RespirationFrontiers in cell and developmental biology · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Mechanisms of mammalian mitochondrial transcription.Protein science : a publication of the Protein Society · 2019
    Review
  13. Article
  14. Review
  15. Organization and dynamics of yeast mitochondrial nucleoids.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017
    Review
  16. Mitochondrial transcription in mammalian cells.Frontiers in bioscience (Landmark edition) · 2017
    Review
  17. Article
  18. Article
  19. Mitochondrial transcript maturation and its disorders.Journal of inherited metabolic disease · 2015
    Review
  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

3 authors at 1 institution in 1 country.

Zhibo WangDepartment of Pathology, Yale University School of Medicine, New Haven, Connecticut 06520-8023, USA.
Justin Cotney
Gerald S Shadel
Yale University · US

Funding

Nuclear Control of Mitochondrial Gene ExpressionR01HL059655 · NHLBI · YALE UNIVERSITY · PI SHADEL, GERALD · 1997 to 2011
$3.1M
NHLBI NIH HHS HO-059655NHLBI NIH HHS R01 HL059655
6 · The paper itself

Abstract

The core human mitochondrial transcription machinery comprises a single subunit bacteriophage-related RNA polymerase, POLRMT, the high mobility group box DNA-binding protein h-mtTFA/TFAM, and two transcriptional co-activator proteins, h-mtTFB1 and h-mtTFB2 that also have rRNA methyltransferase activity. Recapitulation of specific initiation of transcription in vitro can be achieved by a complex of POL-RMT, h-mtTFA, and either h-mtTFB1 or h-mtTFB2. However, the nature of mitochondrial transcription complexes in vivo and the potential involvement of additional proteins in the transcription process in human mitochondria have not been extensively investigated. In Saccharomyces cerevisiae, transcription and translation are physically coupled via the formation of a multiprotein complex nucleated by the binding of Nam1p to the amino-terminal domain of mtRNA polymerase (Rpo41p). This model system paradigm led us to search for proteins that interact with POLRMT to regulate mitochondrial gene expression in humans. Using an affinity capture strategy to identify POL-RMT-binding proteins, we identified mitochondrial ribosomal protein L7/L12 (MRPL12) as a protein in HeLa mitochondrial extracts that interacts specifically with POLRMT in vitro. Purified recombinant MRPL12 binds to POLRMT and stimulates mitochondrial transcription activity in vitro, demonstrating that this interaction is both direct and functional. Finally, from HeLa cells that overexpress FLAG epitope-tagged MRPL12, increased steady-state levels of mtDNA-encoded transcripts are observed and MRPL12-POLRMT complexes can be co-immunoprecipitated, providing strong evidence that this interaction enhances mitochondrial transcription or RNA stability in vivo. We speculate that the MRPL12 interaction with POLRMT is likely part of a novel regulatory mechanism that coordinates mitochondrial transcription with translation and/or ribosome biogenesis during human mitochondrial gene expression.

Indexed as

Cell Cycle ProteinsDNA-Directed RNA PolymerasesGene Expression RegulationHeLa CellsHumansMitochondriaMitochondrial ProteinsNuclear ProteinsProtein BindingProtein BiosynthesisRibosomal ProteinsRibosomesRNA StabilitySaccharomyces cerevisiaeTranscription FactorsTranscription, GeneticCell Cycle ProteinsDNA-Directed RNA PolymerasesMitochondrial ProteinsMRPL12 protein, humanNuclear ProteinsPOLRMT protein, humanRibosomal ProteinsTranscription Factors

Identifiers

PMID17337445
PMCPMC2606046
OpenAlexW2017284374

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.