Evidence map›Paper›PMID 34713605›Full record

ArticleMicrobiologyOpen2021

A hunt for OM45 synthetic petite interactions in Saccharomyces cerevisiae reveals a role for Miro GTPase Gem1p in cristae structure maintenance.

Antonina Shvetsova, Ali J Masud, Laura Schneider, Ulrich Bergmann, Geoffray Monteuuis, Ilkka J Miinalainen, J Kalervo Hiltunen, Alexander J Kastaniotis

Abstract read
In one paragraph

Article in MicrobiologyOpen, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Hyphal Growth inMicrobiology spectrum · 2023
    Article
  2. 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

8 authors.

Antonina ShvetsovaFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.
Ali J MasudFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0002-4126-6513
Laura SchneiderFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.
Ulrich BergmannFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0002-8684-9640
Geoffray MonteuuisFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0001-7193-7771
Ilkka J MiinalainenFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.
J Kalervo HiltunenFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0002-3073-9602
Alexander J KastaniotisFaculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland.ORCID 0000-0003-3624-9214

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Om45 is a major protein of the yeast's outer mitochondrial membrane under respiratory conditions. However, the cellular role of the protein has remained obscure. Previously, deletion mutant phenotypes have not been found, and clear amino acid sequence similarities that would allow inferring its functional role are not available. In this work, we describe synthetic petite mutants of GEM1 and UGO1 that depend on the presence of OM45 for respiratory growth, as well as the identification of several multicopy suppressors of the synthetic petite phenotypes. In the analysis of our mutants, we demonstrate that Om45p and Gem1p have a collaborative role in the maintenance of mitochondrial morphology, cristae structure, and mitochondrial DNA maintenance. A group of multicopy suppressors rescuing the synthetic lethal phenotypes of the mutants on non-fermentable carbon sources additionally supports this result. Our results imply that the synthetic petite phenotypes we observed are due to the disturbance of the inner mitochondrial membrane and point to this mitochondrial sub-compartment as the main target of action of Om45p, Ugo1p, and the yeast Miro GTPase Gem1p.

Indexed as

DNA, FungalDNA, MitochondrialGTP PhosphohydrolasesMembrane ProteinsMitochondriaMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA, FungalDNA, MitochondrialGEM1 protein, S cerevisiaeGTP PhosphohydrolasesMembrane ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsOm45 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUGO1 protein, S cerevisiaecristae organizationGEM1Miro GTPasemitochondriamtDNA inheritanceOM45outer and inner mitochondrial membranesUGO1

Identifiers

PMID34713605
PMCPMC8501180

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.