ArticlePlant physiology2004
A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 117 citations in OpenAlex.
- Functional Interaction Between Toc75 POTRA1 Domain and Tic22-III in the Intermembrane Space During Chloroplast Protein Import.Plant direct · 2026Article
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- Plastid caseinolytic protease OsClpR1 regulates chloroplast development and chloroplast RNA editing in rice.Rice (New York, N.Y.) · 2021Article
- OsNBL1, a Multi-Organelle Localized Protein, Plays Essential Roles in Rice Senescence, Disease Resistance, and Salt Tolerance.Rice (New York, N.Y.) · 2021Article
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- Protective Roles of Cytosolic and Plastidal Proteasomes on Abiotic Stress and Pathogen Invasion.Plants (Basel, Switzerland) · 2020Review
- Protein Import Motors in Chloroplasts: On the Role of Chaperones.The Plant cell · 2020Article
- Origins, function, and regulation of the TOC-TIC general protein import machinery of plastids.Journal of experimental botany · 2020Article
- Co-Suppression ofPlants (Basel, Switzerland) · 2020Article
- Co-suppression of NbClpC1 and NbClpC2 alters plant morphology with changed hormone levels in Nicotiana benthamiana.Plant cell reports · 2019Article
- The TOC GTPase Receptors: Regulators of the Fidelity, Specificity and Substrate Profiles of the General Protein Import Machinery of Chloroplasts.The protein journal · 2019Review
- A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019Article
- The caseinolytic protease complex component CLPC1 in Arabidopsis maintains proteome and RNA homeostasis in chloroplasts.BMC plant biology · 2018Article
- The integration of chloroplast protein targeting with plant developmental and stress responses.BMC biology · 2017Review
- Generation and characterization of a collection of knock-down lines for the chloroplast Clp protease complex in tobacco.Journal of experimental botany · 2017Article
- Crystal structures reveal N-terminal Domain of Arabidopsis thaliana ClpD to be highly divergent from that of ClpC1.Scientific reports · 2017Article
- Chloroplast Hsp93 Directly Binds to Transit Peptides at an Early Stage of the Preprotein Import Process.Plant physiology · 2016Article
- Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.Plant physiology · 2016Article
- GUN1, a Jack-Of-All-Trades in Chloroplast Protein Homeostasis and Signaling.Frontiers in plant science · 2016Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular chaperones are required for the translocation of many proteins across organellar membranes, presumably by providing energy in the form of ATP hydrolysis for protein movement. In the chloroplast protein import system, a heat shock protein 100 (Hsp100), known as Hsp93, is hypothesized to be the chaperone providing energy for precursor translocation, although there is little direct evidence for this hypothesis. To learn more about the possible function of Hsp93 during protein import into chloroplasts, we isolated knockout mutant lines that contain T-DNA disruptions in either atHSP93-V or atHSP93-III, which encode the two Arabidopsis (Arabidopsis thaliana) homologs of Hsp93. atHsp93-V mutant plants are much smaller and paler than wild-type plants. In addition, mutant chloroplasts contain less thylakoid membrane when compared to the wild type. Plastid protein composition, however, seems to be largely unaffected in atHsp93-V knockout plants. Chloroplasts isolated from the atHsp93-V knockout mutant line are still able to import a variety of precursor proteins, but the rate of import of some of these precursors is significantly reduced. These results indicate that atHsp93-V has an important, but not essential, role in the biogenesis of Arabidopsis chloroplasts. In contrast, knockout mutant plants for atHsp93-III, the second Arabidopsis Hsp93 homolog, had a visible phenotype identical to the wild type, suggesting that atHsp93-III may not play as important a role as atHsp93-V in chloroplast development and/or function.
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