ArticlePlant physiology2016
Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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.
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.
Who cites it
35 citing papers in PubMed, 56 citations in OpenAlex.
- Dual Cytoplasmic and Chloroplastic Mechanisms Fine-Tune Chloroplast Division through ARC3 Protein Stability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Functional Interaction Between Toc75 POTRA1 Domain and Tic22-III in the Intermembrane Space During Chloroplast Protein Import.Plant direct · 2026Article
- Correlated Evolutionary Rates Reveal Novel Components and Cross-Compartment Connectivity in Plant Proteostasis Systems.Genome biology and evolution · 2026Article
- Proteostasis and protein quality control in chloroplasts: mechanisms and novel insights related to protein mislocalization.Journal of experimental botany · 2025Review
- Chloroplast precursor protein preClpD overaccumulation triggers multilevel reprogramming of gene expression and a heat shock-like response.Nature communications · 2025Article
- Targeting signals required for protein sorting to sub-chloroplast compartments.Plant cell reports · 2024Review
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Silencing an ATP-Dependent Caseinolytic Protease Proteolytic Subunit Gene Enhances the Resistance of Rice toInternational journal of molecular sciences · 2024Article
- 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 · 2023Article
- Multiple ubiquitin E3 ligase genes antagonistically regulate chloroplast-associated protein degradation.Current biology : CB · 2023Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- Chloroplasts Protein Quality Control and Turnover: A Multitude of Mechanisms.International journal of molecular sciences · 2022Review
- Plastid chaperone HSP90C guides precursor proteins to the SEC translocase for thylakoid transport.Journal of experimental botany · 2020Article
- Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.The Plant cell · 2020Article
- Integrated Analysis of Small RNA, Transcriptome, and Degradome Sequencing Reveals the Water-Deficit and Heat Stress Response Network in Durum Wheat.International journal of molecular sciences · 2020Article
- Protein Import Motors in Chloroplasts: On the Role of Chaperones.The Plant cell · 2020Article
- Protein import into chloroplasts and its regulation by the ubiquitin-proteasome system.Biochemical Society transactions · 2020Review
- Co-Suppression ofPlants (Basel, Switzerland) · 2020Article
- Extensive Posttranscriptional Regulation of Nuclear Gene Expression by Plastid Retrograde Signals.Plant physiology · 2019Article
- Proteomic Analysis of ArabidopsisFrontiers in plant science · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The Hsp100-type chaperone Hsp93/ClpC has crucial roles in chloroplast biogenesis. In addition to its role in proteolysis in the stroma, biochemical and genetic evidence led to the hypothesis that this chaperone collaborates with the inner envelope TIC complex to power preprotein import. Recently, it was suggested that Hsp93, working together with the Clp proteolytic core, can confer a protein quality control mechanism at the envelope. Thus, the role of envelope-localized Hsp93, and the mechanism by which it participates in protein import, remain unclear. To analyze the function of Hsp93 in protein import independently of its ClpP association, we created a mutant of Hsp93 affecting its ClpP-binding motif (PBM) (Hsp93[P-]), which is essential for the chaperone's interaction with the Clp proteolytic core. The Hsp93[P-] construct was ineffective at complementing the pale-yellow phenotype of hsp93 Arabidopsis (Arabidopsis thaliana) mutants, indicating that the PBM is essential for Hsp93 function. As expected, the PBM mutation negatively affected the degradation activity of the stromal Clp protease. The mutation also disrupted association of Hsp93 with the Clp proteolytic core at the envelope, without affecting the envelope localization of Hsp93 itself or its association with the TIC machinery, which we demonstrate to be mediated by a direct interaction with Tic110. Nonetheless, Hsp93[P-] expression did not detectably improve the protein import efficiency of hsp93 mutant chloroplasts. Thus, our results do not support the proposed function of Hsp93 in protein import propulsion, but are more consistent with the notion of Hsp93 performing a quality control role at the point of import.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.