Aug 2026· Comparative Biochemistry and Physiology - Part D:Genomics and Proteomics· Vol 60, pp.
101982
· 0 citations· 30 references
Medicine
TL;DR
A genome-wide analysis of the HSP gene family is performed to provide a genomic framework for HSP genes in L. vannamei and identify candidate genes and variants associated with thermal stress responses.
Abstract
Heat shock proteins (HSPs) are conserved molecular chaperones involved in protein folding, refolding, aggregation prevention, and degradation of damaged proteins. However, the genomic organization and thermal responsiveness of HSP genes in the Pacific white shrimp (Litopenaeus vannamei) remain incompletely understood. Here, we performed a genome-wide analysis of the HSP gene family and examined its phylogenetic relationships, structural features, duplication patterns, sequence variation, interaction networks, and transcriptional responses to acute heat stress. A total of 34 HSP genes were identified and classified into the HSP90, HSP70, HSP40/DNAJ, HSP60, and small HSP families. Phylogenetic, motif, gene structure, synteny, and subcellular localization analyses revealed evolutionary conservation and structural diversification among family members. Three duplicated gene pairs were identified, comprising two segmental duplications and one tandem duplication. All pairs exhibited Ka/Ks ratios below 1, consistent with purifying selection of varying strength. Sequence analysis identified 295 nonsynonymous single-nucleotide polymorphisms, of which 12 were consistently predicted to be deleterious by multiple algorithms. Protein-protein interaction analysis indicated enrichment of protein-folding and cellular stress-response functions. RT-qPCR analysis showed significant induction of HSPA4, HSP90AA1, TRAP1, BiP, and DNAJA1 after 6, 12, and 24 h of exposure to 34 °C, whereas DNAJC3 was significantly induced only at 12 h. All six genes reached their highest transcript abundance at 12 h. These findings may provide a genomic framework for HSP genes in L. vannamei and identify candidate genes and variants associated with thermal stress responses.
A genome-wide identification and comparative analysis of the CSP gene family in yak is performed primarily using bioinformatics approaches based on publicly available genomic and transcriptomic datasets, along with a preliminary validation of their differential expression under cold and hypoxic stress.
The key marker genes and in silico interaction networks identified herein provide a robust resource for functional characterization and molecular breeding to improve stress resilience in zucchini.
Kevser Ceylan, M. Baloğlu, Y. Ceylan et al.· Plant growth regulation (Pri...· 0 citations
The results indicate that PvHsp90 genes are evolutionarily conserved and differentially regulated during heat stress, highlighting PvHsp90‑1 and PvHsp90‑2 as promising candidates for improving reproductive thermotolerance and heat resilience in common bean.
Bayram Ali Yerlikaya, Batuhan Gül, Seher Yerlikaya· Journal of Crop Health· 0 citations
Heat shock proteins (HSPs) are essential for cellular homeostasis and thermal adaptation, yet their interaction networks and regulatory mechanisms under high temperature stress remain largely unexplored in aquatic organisms. Here, the expression profiles of HSPs in Urechis unicinctus under high temperature stress were systematically characterized. Among 85 identified HSPs, a member of the HSP70 family, HSP70CA2, was selected for further study due to its sustained and significant differential expression. Sequence analysis revealed that HSP70CA2 has an open reading frame (ORF) of 1917 bp, encoding a 638 amino acid protein. Western blotting confirmed a rapid and significant increase in HSP70CA2 protein levels in both body wall and midgut tissues during early high temperature stress, indicating its active involvement in the initial stress response. Crucially, five novel interacting proteins of HSP70CA2 were screened and identified as cytoskeletal (CIFP), membrane repair (ANXA7), ER-associated (CRT-like), and chaperone (HSP90A1, HSPA8) factors by pull-down assays coupled with LC-MS. These interactions were validated by point to point yeast two-hybrid assays. Our findings suggest that HSP70CA2 acts as an early chaperone related responder associated with cytoskeletal maintenance, membrane repair, and protein folding processes during the acute heat shock response in U. unicinctus. This study provides new evidence for the involvement of a single HSP70 member in multiple cellular protective processes in an aquatic invertebrate, offering fundamental insights into thermal stress adaptation and a potential target for thermotolerance breeding.
Heat shock proteins (HSPs) maintain cellular homeostasis and regulate immune responses across species. HSP90 stabilises and activates regulatory proteins, while HSP70 facilitates protein folding and prevents aggregation. In this study, the complete cDNA sequences of Dastarcus helophoroides - HSP70, HSP90, and β-actin (used as a reference for real-time quantitative polymerase chain reaction) - were obtained using rapid amplification of cDNA ends-polymerase chain reaction, and the expression of HSP70 and HSP90 under cold stress was analysed. The full-length cDNA of HSP90 contains a 2346-bp open reading frame (ORF) encoding 781 amino acids with a molecular weight (MW) of 89.6 kDa. The HSP70 cDNA contains a 1911-bp ORF encoding 636 amino acids (MW: 69.7 kDa), and the β-actin cDNA contains a 1131-bp ORF encoding 376 amino acids (MW: 41.7 kDa). Cold stress significantly affected HSP expression: HSP90 expression peaked at -15 °C, with a 9.45-fold increase compared to the control (P < 0.05), whereas HSP70 expression increased markedly at -10 °C, with a 60.42-fold increase compared to the control (P < 0.05). These findings have important biological implications for predicting insect performance under fluctuating thermal environments and for optimising low-temperature storage and release strategies of D. helophoroides in biological control programmes.
Yanchen Wang, Defu Chi· Bulletin of entomological re...· 0 citations
The compact size of the SnRK2 family, conserved structural features, and distinct tissue-specific drought response patterns are consistent with a streamlined stress signaling system that may contribute to the ecological adaptation of Bombax ceiba in seasonally dry tropical environments, although formal evolutionary analyses are required to establish adaptive significance.
Yu-Mei Shi, Zhifang Zhang, Ruoxin He et al.· Frontiers in Plant Science· 0 citations
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