Evidence map›Paper›PMID 18216280›Full record

ArticleMolecular biology of the cell2008

ATP25, a new nuclear gene of Saccharomyces cerevisiae required for expression and assembly of the Atp9p subunit of mitochondrial ATPase.

Xiaomei Zeng, Mario H Barros, Theodore Shulman, Alexander Tzagoloff

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Article
  12. Assembling the mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. INA complex liaises the FNature communications · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Modular assembly of yeast cytochrome oxidase.Molecular biology of the cell · 2013
    Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Xiaomei ZengDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Mario H Barros
Theodore Shulman
Alexander Tzagoloff
Columbia University · US

Funding

ASSEMBLY OF MEMBRANES IN HEART AND YEAST MITOCHONDRIAR01HL022174 · NHLBI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TZAGOLOFF, ALEXANDER A · 1985 to 2014
$3.3M
Assembly of membranes in heart and yeast mitochondriaR56HL022174 · NHLBI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TZAGOLOFF, ALEXANDER A · 2009 to 2009
$322k
ASSEMBLY OF MEMBRANES IN HEART &YEAST MITOCHONDRIAR37HL022174 · NHLBI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TZAGOLOFF, ALEXANDER A · 1987 to 1996
–
NHLBI NIH HHS HL-22174NHLBI NIH HHS R01 HL022174NHLBI NIH HHS R56 HL022174
6 · The paper itself

Abstract

We report a new nuclear gene, designated ATP25 (reading frame YMR098C on chromosome XIII), required for expression of Atp9p (subunit 9) of the Saccharomyces cerevisiae mitochondrial proton translocating ATPase. Mutations in ATP25 elicit a deficit of ATP9 mRNA and of its translation product, thereby preventing assembly of functional F(0). Unlike Atp9p, the other mitochondrial gene products, including ATPase subunits Atp6p and Atp8p, are synthesized normally in atp25 mutants. Northern analysis of mitochondrial RNAs in an atp25 temperature-sensitive mutant confirmed that Atp25p is required for stability of the ATP9 mRNA. Atp25p is a mitochondrial inner membrane protein with a predicted mass of 70 kDa. The primary translation product of ATP25 is cleaved in vivo after residue 292 to yield a 35-kDa C-terminal polypeptide. The C-terminal half of Atp25p is sufficient to stabilize the ATP9 mRNA and restore synthesis of Atp9p. Growth on respiratory substrates, however, depends on both halves of Atp25p, indicating that the N-terminal half has another function, which we propose to be oligomerization of Atp9p into a proper size ring structure.

Indexed as

Genes, FungalAllelesBase SequenceCell NucleusCloning, MolecularDNA, FungalGene ExpressionGenetic Complementation TestMitochondrial Proton-Translocating ATPasesMolecular WeightMutationProtein SubunitsRecombinant ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiaeDNA, FungalMitochondrial Proton-Translocating ATPasesOLI1 protein, S cerevisiaeProtein SubunitsRecombinant ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID18216280
PMCPMC2291438
OpenAlexW2049199326

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.