ArticleJournal of experimental botany2015
A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein 90 is required for resistance to tunicamycin or high calcium-induced ER stresses.
Article in Journal of experimental botany, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Identification of thePlants (Basel, Switzerland) · 2025Article
- HSP90 interacts with VP37 to facilitate the cell-to-cell movement of broad bean wilt virus 2.mBio · 2025Article
- Secretion of a low-molecular-weight species of endogenous GRP94 devoid of the KDEL motif during endoplasmic reticulum stress in Chinese hamster ovary cells.Traffic (Copenhagen, Denmark) · 2021Article
- Comparative analysis of developing grain transcriptome reveals candidate genes and pathways improving GPC in wheat lines derived from wild emmer.Journal of applied genetics · 2021Article
- Genome-Wide Identification and Characterization of HSP90-RAR1-SGT1-Complex Members FromFrontiers in genetics · 2021Article
- Sexual and Apogamous Species of Woodferns Show Different Protein and Phytohormone Profiles.Frontiers in plant science · 2021Article
- Elucidating Drought Stress Tolerance in European Oaks Through Cross-Species Transcriptomics.G3 (Bethesda, Md.) · 2019Article
- Identification of AtHsp90.6 involved in early embryogenesis and its structure prediction by molecular dynamics simulations.Royal Society open science · 2019Article
- An E. coli biosensor for screening of cDNA libraries for isochorismate pyruvate lyase-encoding cDNAs.Molecular genetics and genomics : MGG · 2018Article
- Protein Quality Control in the Endoplasmic Reticulum of Plants.Annual review of plant biology · 2018Review
- Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.Cell reports · 2017Article
- Maintaining the factory: the roles of the unfolded protein response in cellular homeostasis in plants.The Plant journal : for cell and molecular biology · 2017Article
- A comparative study on Ca content and distribution in two Gesneriaceae species reveals distinctive mechanisms to cope with high rhizospheric soluble calcium.Frontiers in plant science · 2014Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock protein 90 (HSP90) is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes under both physiological and stress conditions. In Arabidopsis, there are seven HSP90 isoforms (HSP90.1-HSP90.7) that are localized in the cytoplasm/nucleus, mitochondrion, chloroplast, and endoplasmic reticulum (ER) where protein folding actively takes place. In this study, we analysed the sequence of ER-localized Arabidopsis HSP90.7 and the other ER GRP94 proteins from plants and animals, and identified a short, charged region that is specifically present in the middle domain of plant-derived GRP94 proteins. To understand the role of this charged region, we analysed transgenic plants that expressed a mutant protein, HSP90.7(Δ22), which had this charged region deleted. We showed that seedlings expressing HSP90.7(Δ22) had significantly enhanced sensitivity to ER stress induced by tunicamycin or a high concentration of calcium, although its general chaperone activity in preventing the model protein from heat-induced aggregation was not significantly affected. We also analysed the ATP-binding and hydrolysis activity of both wild-type and mutant HSP90.7 proteins, and found that they had slightly different ATP-binding affinities. Finally, using a yeast two-hybrid screen, we identified a small set of HSP90.7 interactors and showed that the charged region is not required for the candidate client interaction, although it may affect their binding affinity, thus providing potential targets for further investigation of HSP90.7 functions.
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