Evidence map›Paper›PMID 27288365›Full record

ReviewPlant physiology2016

Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments.

Kenji Nishimura, Yusuke Kato, Wataru Sakamoto

Open access · greenAbstract readReview
In one paragraph

Review in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

83 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Rapid COThe Plant journal : for cell and molecular biology · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Proteomic analysis of unicellular cyanobacteriumbioRxiv : the preprint server for biology · 2024
    Article
  20. Article

23 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Kenji NishimuraInstitute of Plant Science and Resources, Okayama University, Kurashiki, Okayama 710-0046, Japan.
Yusuke KatoInstitute of Plant Science and Resources, Okayama University, Kurashiki, Okayama 710-0046, Japan.ORCID 0000-0003-1718-9121
Wataru SakamotoInstitute of Plant Science and Resources, Okayama University, Kurashiki, Okayama 710-0046, Japan saka@okayama-u.ac.jp.ORCID 0000-0001-9747-5042
Okayama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplasts originated from the endosymbiosis of ancestral cyanobacteria and maintain transcription and translation machineries for around 100 proteins. Most endosymbiont genes, however, have been transferred to the host nucleus, and the majority of the chloroplast proteome is composed of nucleus-encoded proteins that are biosynthesized in the cytosol and then imported into chloroplasts. How chloroplasts and the nucleus communicate to control the plastid proteome remains an important question. Protein-degrading machineries play key roles in chloroplast proteome biogenesis, remodeling, and maintenance. Research in the past few decades has revealed more than 20 chloroplast proteases, which are localized to specific suborganellar locations. In particular, two energy-dependent processive proteases of bacterial origin, Clp and FtsH, are central to protein homeostasis. Processing endopeptidases such as stromal processing peptidase and thylakoidal processing peptidase are involved in the maturation of precursor proteins imported into chloroplasts by cleaving off the amino-terminal transit peptides. Presequence peptidases and organellar oligopeptidase subsequently degrade the cleaved targeting peptides. Recent findings have indicated that not only intraplastidic but also extraplastidic processive protein-degrading systems participate in the regulation and quality control of protein translocation across the envelopes. In this review, we summarize current knowledge of the major chloroplast proteases in terms of type, suborganellar localization, and diversification. We present details of these degradation processes as case studies according to suborganellar compartment (envelope, stroma, and thylakoids). Key questions and future directions in this field are discussed.

Indexed as

ProteolysisArabidopsisArabidopsis ProteinsCell NucleusChloroplastsEndopeptidasesHomeostasisMetalloendopeptidasesModels, MolecularPeptide HydrolasesPlant ProteinsProtein TransportProteomeThylakoidsArabidopsis ProteinsEndopeptidasesMetalloendopeptidasesoligopeptidasePeptide HydrolasesPlant ProteinsProteomestromal processing peptidasethylakoid processing peptidase

Identifiers

PMID27288365
PMCPMC4972267
OpenAlexW2415130743

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.