Evidence map›Paper›PMID 34608962›Full record

ArticlePlant physiology2021

FTSH4 and OMA1 mitochondrial proteases reduce moderate heat stress-induced protein aggregation.

Agata Maziak, Malgorzata Heidorn-Czarna, Aleksandra Weremczuk, Hanna Janska

Abstract read
In one paragraph

Article in Plant physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Plants (Basel, Switzerland) · 2024
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  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.

Agata MaziakDepartment of Cellular Molecular Biology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, 50-383, Poland.ORCID 0000-0002-7238-8150
Malgorzata Heidorn-CzarnaDepartment of Cellular Molecular Biology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, 50-383, Poland.ORCID 0000-0003-0850-2681
Aleksandra WeremczukDepartment of Cellular Molecular Biology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, 50-383, Poland.ORCID 0000-0002-5228-1874
Hanna JanskaDepartment of Cellular Molecular Biology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, 50-383, Poland.ORCID 0000-0002-6542-343X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The threat of global warming makes uncovering mechanisms of plant tolerance to long-term moderate heat stress particularly important. We previously reported that Arabidopsis (Arabidopsis thaliana) plants lacking mitochondrial proteases FTSH4 or OMA1 suffer phenotypic changes under long-term stress of 30°C, while their growth at 22°C is not affected. Here we found that these morphological and developmental changes are associated with increased accumulation of insoluble mitochondrial protein aggregates that consist mainly of small heat-shock proteins (sHSPs). Greater accumulation of sHSPs in ftsh4 than oma1 corresponds with more severe phenotypic abnormalities. We showed that the proteolytic activity of FTSH4, and to a lesser extent of OMA1, as well as the chaperone function of FTSH4, is crucial for protecting mitochondrial proteins against aggregation. We demonstrated that HSP23.6 and NADH dehydrogenase subunit 9 present in aggregates are proteolytic substrates of FTSH4, and this form of HSP23.6 is also a substrate of OMA1 protease. In addition, we found that the activity of FTSH4 plays an important role during recovery from elevated to optimal temperatures. Isobaric tags for relative and absolute quantification (iTRAQ)-based proteomic analyses, along with identification of aggregation-prone proteins, implicated mitochondrial pathways affected by protein aggregation (e.g. assembly of complex I) and revealed that the mitochondrial proteomes of ftsh4 and oma1 plants are similarly adapted to long-term moderate heat stress. Overall, our data indicate that both FTSH4 and OMA1 increase the tolerance of plants to long-term moderate heat stress by reducing detergent-tolerant mitochondrial protein aggregation.

Indexed as

ArabidopsisArabidopsis ProteinsHeat-Shock ResponseMetalloproteasesMitochondrial ProteinsArabidopsis ProteinsFtsH4 protein, ArabidopsisMetalloproteasesMitochondrial Proteins

Identifiers

PMID34608962
PMCPMC8491029

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.