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The translation initiation factor eIF3M2 upregulates HEAT SHOCK PROTEIN 70 to maintain pollen tube membrane integrity during heat shock.
Plant Physiol
December 2024
Laboratory of Pollen Biology, Institute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 00 Prague 6, Czech Republic.
Pollen germination and pollen tube (PT) growth are extremely sensitive to high temperatures. During heat stress (HS), global translation shuts down and favors the maintenance of the essential cellular proteome for cell viability and protection against protein misfolding. Here, we demonstrate that under normal conditions, the Arabidopsis (Arabidopsis thaliana) eukaryotic translation initiation factor subunit eif3m1/eif3m2 double mutant exhibits poor pollen germination, loss of PT integrity and an increased rate of aborted seeds.
View Article and Find Full Text PDFand Families in : Genome-Wide Identification, Molecular Characterization, and Expression Profiles in Response to Various Environmental Stressors.
Front Physiol
November 2021
Key Laboratory of Mariculture, Ocean University of China, Ministry of Education, Qingdao, China.
Heat shock proteins (HSPs) are a large class of highly conserved chaperons, which play important roles in response to elevated temperature and other environmental stressors. In the present study, 5 genes and 17 genes were systematically characterized in spotted seabass (). The evolutionary footprint of genes was revealed via the analysis of phylogeny, chromosome location, and gene copy numbers.
View Article and Find Full Text PDFA heat-shock response regulated by the PfAP2-HS transcription factor protects human malaria parasites from febrile temperatures.
Nat Microbiol
September 2021
ISGlobal, Hospital Clínic-Universitat de Barcelona, Barcelona, Spain.
Periodic fever is a characteristic clinical feature of human malaria, but how parasites survive febrile episodes is not known. Although the genomes of Plasmodium species encode a full set of chaperones, they lack the conserved eukaryotic transcription factor HSF1, which activates the expression of chaperones following heat shock. Here, we show that PfAP2-HS, a transcription factor in the ApiAP2 family, regulates the protective heat-shock response in Plasmodium falciparum.
View Article and Find Full Text PDFIntravenous Immunoglobulin G Suppresses Heat Shock Protein (HSP)-70 Expression and Enhances the Activity of HSP90 and Proteasome Inhibitors.
Front Immunol
April 2021
Department of Lymphoma and Myeloma, The University of Texas MD Anderson Cancer Center, Houston, TX, United States.
Article Synopsis
- Intravenous immunoglobulin G (IVIgG) is primarily approved for treating primary immunodeficiency, but it also shows potential anti-cancer effects, especially in multiple myeloma and mantle cell lymphoma (MCL).
- The study found that IVIgG inhibits the growth of various cancer cells, induces cell cycle arrest, and suppresses key pro-tumor cytokines while reducing HSP70-1 levels and blocking the transfer of drug resistance via extracellular vesicles.
- Combining IVIgG with the HSP90 inhibitor AUY922 or proteasome inhibitors like bortezomib enhances its effectiveness against resistant cancer cells, suggesting that the anti-HSP70-1 IgG in IVIgG could
A subclass of HSP70s regulate development and abiotic stress responses in Arabidopsis thaliana.
J Plant Res
March 2017
State Key Laboratory of Genetic Engineering and Institute of Plant Biology, School of Life Sciences, Fudan University, Room 421, School of Life Science Building, No. 2005, Songhu Road, Shanghai, 200438, China.
Members of the HSP70 family function as molecular chaperones to maintain cellular homeostasis and help plants cope with environmental stimuli. However, due to functional redundancy and lack of effective chemical inhibitors, our knowledge of functions of individual HSP70s has remained limited. Here, we confirmed a subclass of HSP70s, including HSP70-1, -2, -3, -4, and -5, localized to the cytosol and nucleus in Arabidopsis thaliana.
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