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The small heat shock proteins (sHSPs) are a diverse family of molecular chaperones. It is well established that these proteins are crucial components of the plant heat shock response. They also have important roles in other stress responses and in normal development. We have conducted a comparative sequence analysis of the sHSPs in three complete angiosperms genomes: Arabidopsis thaliana, Populus trichocarpa, and Oryza sativa. Our phylogenetic analysis has identified four additional plant sHSP subfamilies and thus has increased the number of plant sHSP subfamilies from 7 to 11. We have also identified a number of novel sHSP genes in each genome that lack close homologs in other genomes. Using publicly available gene expression data and predicted secondary structures, we have determined that the sHSPs in plants are far more diverse in sequence, expression profile, and in structure than had been previously known. Some of the newly identified subfamilies are not stress regulated, may not possess the highly conserved large oligomer structure, and may not even function as molecular chaperones. We found no consistent evolutionary patterns across the three species studied. For example, gene conversion was found among the sHSPs in O. sativa but not in A. thaliana or P. trichocarpa. Among the three species, P. trichocarpa had the most sHSPs. This was due to an expansion of the cytosolic I sHSPs that was not seen in the other two species. Our analysis indicates that the sHSPs are a dynamic protein family in angiosperms with unexpected levels of diversity.
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http://dx.doi.org/10.1007/s12192-008-0023-7 | DOI Listing |
Mol Biol Rep
September 2025
Laboratory of Genomic Research, Research Institute for Genetic and Molecular Epidemiology, Kursk State Medical University, Kursk, 305041, Russia.
Background: The chaperoning system, which is responsible for protein homeostasis, plays a significant role in cardiovascular diseases. Among molecular chaperones or heat shock proteins (HSPs), the HSP40 family, the main co-chaperone of HSP70, remains largely underexplored, especially in ischemic heart disease (IHD) risk.
Materials And Results: We genotyped 834 IHD patients and 1,328 healthy controls for three SNPs (rs2034598 and rs7189628 DNAJA2 and rs4926222 DNAJB1) using probe-based real-time PCR.
FEMS Yeast Res
September 2025
Department of Bioengineering, School of Life Science Engineering, College of Interdisciplinary Science and Technology, University of Tehran, Tehran, Iran.
The growing challenges posed by global warming and the demand for sustainable food and feed resources underscore the need for robust microbial platforms in bioprocessing. Thermotolerant yeasts have emerged as promising candidates due to their ability to thrive at elevated temperatures and other industrially relevant stresses. This review examines the industrial potential of thermotolerant yeasts in the context of climate change, emphasizing how their resilience can lead to more energy-efficient and cost-effective bioprocesses.
View Article and Find Full Text PDFVet World
July 2025
Department of Veterinary Anatomy, Faculty of Veterinary Medicine, Universitas Airlangga, Surabaya, Indonesia.
Background And Aim: Indonesia's indigenous Kacang goat population is in decline, posing a threat to food security and genetic diversity. maturation and cryopreservation techniques are key strategies for genetic conservation. However, heat shock stress during cryopreservation can compromise oocyte viability.
View Article and Find Full Text PDFTemperature (Austin)
April 2025
Department of Health and Human Performance, Texas State University, San Marcos, TX, USA.
A heat tolerance test (HTT) can aid in return-to-play decision making following exertional heat stroke (EHS). The HTT uses rectal temperature (T, >38.5°C) and heart rate thresholds (HR; >150 bpm) to identify "heat intolerance.
View Article and Find Full Text PDFBiomed Pharmacother
September 2025
Department of Biomedical Sciences, Institute of Health, Jimma University, Jimma 378, Ethiopia; Division of Research & Development, Lovely Professional University, Phagwara 144411, India. Electronic address:
Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterised by cognitive decline and the accumulation of misfolded proteins, including amyloid-beta and hyperphosphorylated tau, which impair neuronal function and promote cell death. These misfolded proteins disrupt proteostasis by forming toxic aggregates that exacerbate disease progression. Molecular chaperones, such as heat shock proteins, actively maintain protein homeostasis by assisting in proper folding, preventing aggregation, and promoting the clearance of misfolded proteins.
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