Evidence map›Paper›PMID 30721974›Full record

ArticleJournal of experimental botany2019

Reduced expression of the proteolytically inactive FtsH members has impacts on the Darwinian fitness of Arabidopsis thaliana.

Laxmi S Mishra, Kati Mielke, Raik Wagner, Christiane Funk

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Genome-Wide Identification and Comprehensive Analysis of theInternational journal of molecular sciences · 2023
    Article
  4. Chloroplast import motor subunits FtsHi1 and FtsHi2 are located on opposite sides of the inner envelope membrane.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. A systematicFrontiers in plant science · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. The FtsHi Enzymes ofInternational journal of molecular sciences · 2021
    Review
  11. Article
  12. Article
  13. The Plastid-Localized AtFtsHi3 Pseudo-Protease ofFrontiers in plant science · 2021
    Article
  14. Article
  15. Plant proteases and programmed cell death.Journal of experimental botany · 2019
    Article
  16. 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.

Laxmi S MishraDepartment of Chemistry, Umeå University, Umeå, Sweden.
Kati MielkeDepartment of Chemistry, Umeå University, Umeå, Sweden.
Raik WagnerDepartment of Chemistry, Umeå University, Umeå, Sweden.
Christiane FunkDepartment of Chemistry, Umeå University, Umeå, Sweden.
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FtsH (filamentation-temperature-sensitive protein H) proteases are a family of membrane-bound enzymes present in eubacteria, animals, and plants. Besides the 12 genes encoding proteolytically active members of the FtsH family in the genome of Arabidopsis, there are five genes coding for members that are assumed to be proteolytically inactive due to mutations in the protease domain; these are termed FtsHi (i for inactive). Despite their lack of proteolytic activity, these FtsHi members seem to be important for chloroplast and plant development as four out of five homozygous knockout-mutants of FtsHis are embryo-lethal. Here, we analysed the Darwinian fitness of weak homozygous (ftshi1,3,4) and heterozygous (ftshi/FTSHi2,4,5) mutants. We compared the growth and development of these mutants to their respective wild-type Arabidopsis plants under controlled laboratory conditions and in the field, and we also evaluated the photosynthetic efficiency by pulse-amplitude modulation fluorescence. Homologous genotypes were subjected to various stress conditions in a greenhouse and gene co-expression as well as phylogenetic analyses were performed. Analysis of the gene-expression network of the five FTSHi genes indicated common clusters with genes encoding FtsH12, OTP51, and methylase. Phylogenetic analyses pointed to a common evolution (and common disappearance in grasses and gymnosperms) of FtsH12 and multiple presumably proteolytically inactive FtsHi enzymes. Our data show that the FtsHi enzymes are highly important during the seedling stage and for Darwinian fitness analyses in semi-natural conditions.

Indexed as

Gene Expression Regulation, PlantGenetic FitnessArabidopsisArabidopsis ProteinsMetalloendopeptidasesMetalloproteasesMutationPhotosynthesisPhylogenyArabidopsis ProteinsFtsH protein, ArabidopsisMetalloendopeptidasesMetalloproteasesAAA-type proteaseembryo lethalfield trialFtsH metalloproteasephenotypeseedling

Identifiers

PMID30721974
PMCPMC6460958
OpenAlexW2912678576

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.