Evidence map›Paper›PMID 24435062›Full record

ArticleNature communications2014

Distinct structural features of TFAM drive mitochondrial DNA packaging versus transcriptional activation.

Huu B Ngo, Geoffrey A Lovely, Rob Phillips, David C Chan

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed
8.7field-weighted citation impact, top 2% 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

160 citing papers in PubMed, 242 citations in OpenAlex.

  1. Article
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  7. TFAM organizes DNA into compact higher order structures.bioRxiv : the preprint server for biology · 2026
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  17. Cytosine methylase and hydroxymethylase activity in mammalian mitochondria.Frontiers in cell and developmental biology · 2025
    Article
  18. Article
  19. Article
  20. Article

100 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Huu B Ngo1] Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125, USA [2] Howard Hughes Medical Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA.
Geoffrey A Lovely1] Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125, USA [2] Department of Applied Physics, California Institute of Technology, Pasadena, California 91125, USA.
Rob Phillips1] Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125, USA [2] Department of Applied Physics, California Institute of Technology, Pasadena, California 91125, USA.
David C Chan1] Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, California 91125, USA [2] Howard Hughes Medical Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA.
California Institute of Technology · US

Funding

NIH Director's Pioneer Award (RMI)DP1OD000217 · OD · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI PHILLIPS, ROB · 2004 to 2008
$4.0M
Mitochondrial Fusion: Analysis of Fzo FunctionR01GM062967 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CHAN, DAVID C · 2001 to 2014
$3.7M
Single-Molecule and Single-Cell Analysis of Transcription Factor-DNA ComplexesR01GM085286 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI PHILLIPS, ROB · 2009 to 2015
$2.8M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM062967NIGMS NIH HHS R01 GM085286NIH HHS DP1 OD000217NIH HHS DP1 OD000217A
6 · The paper itself

Abstract

TFAM (transcription factor A, mitochondrial) is a DNA-binding protein that activates transcription at the two major promoters of mitochondrial DNA (mtDNA)--the light strand promoter (LSP) and the heavy strand promoter 1 (HSP1). Equally important, it coats and packages the mitochondrial genome. TFAM has been shown to impose a U-turn on LSP DNA; however, whether this distortion is relevant at other sites is unknown. Here we present crystal structures of TFAM bound to HSP1 and to nonspecific DNA. In both, TFAM similarly distorts the DNA into a U-turn. Yet, TFAM binds to HSP1 in the opposite orientation from LSP explaining why transcription from LSP requires DNA bending, whereas transcription at HSP1 does not. Moreover, the crystal structures reveal dimerization of DNA-bound TFAM. This dimerization is dispensable for DNA bending and transcriptional activation but is important in DNA compaction. We propose that TFAM dimerization enhances mitochondrial DNA compaction by promoting looping of the DNA.

Indexed as

Base SequenceCrystallizationDimerizationDNADNA-Binding ProteinsDNA, MitochondrialDNA PackagingHumansMitochondrial ProteinsMolecular Sequence DataPromoter Regions, GeneticProtein ConformationSequence Analysis, DNATranscriptional ActivationTranscription FactorsDNADNA-Binding ProteinsDNA, MitochondrialMitochondrial ProteinsTFAM protein, humanTranscription Factors

Identifiers

PMID24435062
PMCPMC3936014
OpenAlexW2056004646

What OpenQuestion holds

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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.