Evidence map›Paper›PMID 17135290›Full record

ArticleMolecular biology of the cell2007

The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase.

Xiaomei Zeng, Walter Neupert, Alexander Tzagoloff

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
3.1field-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

54 citing papers in PubMed, 1 synthesis or guideline pooled it, 103 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. T1121G Point Mutation in the Mitochondrial GeneInternational journal of molecular sciences · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. Atp23p and Atp10p coordinate to regulate the assembly of yeast mitochondrial ATP synthase.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  18. Review
  19. Article
  20. Review
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 2 institutions in 2 countries.

Xiaomei ZengDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Walter Neupert
Alexander Tzagoloff
Columbia University · USLudwig-Maximilians-Universität München · DE

Funding

ASSEMBLY OF MEMBRANES IN HEART AND YEAST MITOCHONDRIAR01HL022174 · NHLBI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TZAGOLOFF, ALEXANDER A · 1985 to 2014
$3.3M
NHLBI NIH HHS HL2274NHLBI NIH HHS R01 HL022174
6 · The paper itself

Abstract

In the present study we have identified a new metalloprotease encoded by the nuclear ATP23 gene of Saccharomyces cerevisiae that is essential for expression of mitochondrial ATPase (F(1)-F(O) complex). Mutations in ATP23 cause the accumulation of the precursor form of subunit 6 and prevent assembly of F(O). Atp23p is associated with the mitochondrial inner membrane and is conserved from yeast to humans. A mutant harboring proteolytically inactive Atp23p accumulates the subunit 6 precursor but is nonetheless able to assemble a functional ATPase complex. These results indicate that removal of the subunit 6 presequence is not an essential event for ATPase biogenesis and that Atp23p, in addition to its processing activity, must provide another important function in F(O) assembly. The product of the yeast ATP10 gene was previously shown to interact with subunit 6 and to be required for its association with the subunit 9 ring. In this study one extra copy of ATP23 was found to be an effective suppressor of an atp10 null mutant, suggesting an overlap in the functions of Atp23p and Atp10p. Atp23p may, therefore, also be a chaperone, which in conjunction with Atp10p mediates the association of subunit 6 with the subunit 9 ring.

Indexed as

Amino Acid SequenceDNA, MitochondrialGenes, FungalMetalloproteasesMitochondriaMitochondrial Proton-Translocating ATPasesMolecular ChaperonesMolecular Sequence DataMutationPhenotypeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSuppression, GeneticAtp10 protein, S cerevisiaeATP23 protein, S cerevisiaeATP6 protein, S cerevisiaeDNA, MitochondrialMetalloproteasesMitochondrial Proton-Translocating ATPasesMolecular ChaperonesSaccharomyces cerevisiae Proteins

Identifiers

PMID17135290
PMCPMC1783785
OpenAlexW2044159297

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.