The HSP/co-chaperone network in environmental cold adaptation of Chilo suppressalis

Fan, Jun; Chang, Guofeng; Li, Zhenzhen; Abouzaid, Mostafa; Du, Xiaoyong; Hull, J. Joe; Ma, Weihua; Lin, Yongjun

doi:10.1016/j.ijbiomac.2021.07.113

Cited by 21 publications

(14 citation statements)

References 50 publications

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“…As the most conserved gene in the HSP family, HSP70 has been extensively studied [ 19 ]. Studies have shown that the HSP70 members have the function of receiving the denatured protein caused by stress and then transporting it to HSP90 for repair to complete the resisting process [ 57 ]. HSP90 is highly conserved in evolution, and plays a crucial role in different cellular processes, especially reflected in signal transduction and gene transcription [ 58 , 59 ].…”

Section: Discussionmentioning

confidence: 99%

Genome-Wide Identification and Analysis of the Heat-Shock Protein Gene Superfamily in Bemisia tabaci and Expression Pattern Analysis under Heat Shock

Zheng

Qin

Yang

et al. 2022

Insects

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The thermal tolerance of Bemisia tabaci MED, an invasive whitefly species with worldwide distribution, plays an important role in its ecological adaptation during the invasion process. Heat-shock proteins (HSPs) are closely related to heat resistance. In this study, 33 Hsps (BtaHsps) were identified based on sequenced genome of B. tabaci MED belonging to six HSP families, among which 22 Hsps were newly identified. The secondary structures of a further 22 BtaHsps were also predicted. The results of RT-qPCR showed that heat shock could affect the expression of 14 of the 22 Hsps newly identified in this study. Among them, the expression level of six Hsps increased under 42 °C treatment. As the unstudied gene, BtaHsp90A3 had the highest increase rate. Therefore, BtaHsp90A3 was chosen for the RNAi test, and silencing BtaHsp90A3 by RNAi decreased the survival rate of adult B. tabaci at 42 °C. The results indicated that only a few Hsps were involved in the thermal tolerance of host whitefly although many Hsps would response under heat stress. This study conducted a more in-depth and comprehensive identification that demonstrates the evolutionary relationship of BtaHsps and illustrates the response of BtaHsps under the influence of thermal stress in B. tabaci MED.

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Section: Discussionmentioning

confidence: 99%

Genome-Wide Identification and Analysis of the Heat-Shock Protein Gene Superfamily in Bemisia tabaci and Expression Pattern Analysis under Heat Shock

Zheng

Qin

Yang

et al. 2022

Insects

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“…Considering the tissue specificity, the temperature tolerance patterns of PcaHSP20 in other tissues still need further investigation. Under genome-wide analysis, many species showed more HSP genes in response to cold treatment than to thermal treatment [31, 58]. However, compared with heat stress, there were fewer PcaHSPs involved in the response to cold stress and with lower expression levels.…”

Section: Discussionmentioning

confidence: 99%

Genome-wide identification and characterization of the HSP gene superfamily in apple snails (Gastropoda: Ampullariidae) and expression analysis under temperature stress

Gao

et al. 2022

Preprint

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Heat shock proteins (HSPs) play important roles in the response to various stresses by being involved in cellular processes as molecular chaperones. Apple snails from the family Ampullariidae are large freshwater gastropods, while several species from the genus Pomacea have been introduced out of their native ranges and became invasive. The recent release of the genomes of four ampullariids (P. canaliculata, P. maculata, Lanistes nyassanus, and Marisa cornuarietis) has opened the opportunity for a comprehensive genome-wide analysis of the HSP superfamily. We identified that the number of HSP genes from P. canaliculata (PcaHSPs) was greater than that from the other three species. A total of 42 PcaHSPs were distributed on 12 chromosomes and were classified into the families of HSP90, HSP70, HSP60, HSP40, HSP20, and HSP10. The HSP70, HSP40 and HSP20 families have multiple members in the four species, but the other HSP families have one to three genes each. Each HSP family formed a monophyletic clade on the phylogenetic trees, except for the HSP40 family. We identified tandem duplication of paralogous genes in PcaHSP70 and PcaHSP20. The RNA-seq data show that the expression profiles of PcaHSPs in different tissues have similar patterns, except that several genes, mainly from PcaHSP20, revealed tissue-specific expression levels. Based on qPCR, we further identified that there were more HSP genes with stronger induction levels in response to hot stress than cold stress. Our findings will be helpful for future studies on stress response and adaptation focusing on HSPs in apple snails.

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“…When the Hsps repair misfolded proteins in a simplified model, Hsp70 initially facilitates the re-folding of hydrophobic residue stretches into their native state together with Hsp40s (Dnajs), whereas Hsp90 catalyzes a step later in protein folding and activation [8,11]. With the possible co-chaperon among Hsp40s, Hsp70s, and Hsp90s, to further excavate their associated regulation, the expression trend and Pearson's correlation coefficient (PCC) of LmHsp40-70-90 genes under alkalinity stress were further investigated.…”

Section: Coordinated Regulation Of Lmhsp Co-chaperones Under Alkalini...mentioning

confidence: 99%

“…Moreover, gene duplication is one of the most essential ways to develop functional divergence through environmental adaptation [42]. Both Hsp90 and Hsp70 function in an ATP-dependent scenario and require the involvement of a proteinnamed activator of Hsp90 ATPase homolog (Hsp90aa1), which interacts with Hsp90 and Hsp70 to stimulate ATPase activity [8,11]. Two putative Hsp90aa1 genes were identified in L. maculatus due to TSGD, while only one (LmHsp90aa1.2) was significantly induced in response to alkalinity (Figure 4B).…”

Section: Evolutionary Dynamics Of Lmhsp Families In L Maculatusmentioning

confidence: 99%

“…For instance, Hsp70 and Hsp40 could interact with a substrate protein and co-chaperones to facilitate the transfer of the substrate to Hsp90 [9,10], while Hsp90 and Hsp70 could also directly collaborate with each other [10]. In contrast, sHsps function independently of ATP so as to prevent the formation of large insoluble protein aggregates [11].…”

Section: Introductionmentioning

confidence: 99%

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Genomic and Transcriptomic Landscape and Evolutionary Dynamics of Heat Shock Proteins in Spotted Sea Bass (Lateolabrax maculatus) under Salinity Change and Alkalinity Stress

Liu

Wang

et al. 2022

Biology

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The heat shock protein (Hsp) superfamily has received accumulated attention because it is ubiquitous and conserved in almost all living organisms and is involved in a wide spectrum of cellular responses against diverse environmental stresses. However, our knowledge about the Hsp co-chaperon network is still limited in non-model organisms. In this study, we provided the systematic analysis of 95 Hsp genes (LmHsps) in the genome of spotted sea bass (Lateolabrax maculatus), an important aquaculture species in China that can widely adapt to diverse salinities from fresh to sea water, and moderately adapt to high alkaline water. Through in silico analysis using transcriptome and genome database, we determined the expression profiles of LmHsps in response to salinity change and alkalinity stress in L. maculatus gills. The results revealed that LmHsps were sensitive in response to alkalinity stress, and the LmHsp40-70-90 members were more actively regulated than other LmHsps and may also be coordinately interacted as co-chaperons. This was in accordance with the fact that members of LmHsp40, LmHsp70, and LmHsp90 evolved more rapidly in L. maculatus than other teleost lineages with positively selected sites detected in their functional domains. Our results revealed the diverse and cooperated regulation of LmHsps under alkaline stress, which may have arisen through the functional divergence and adaptive recruitment of the Hsp40-70-90 co-chaperons and will provide vital insights for the development of L. maculatus cultivation in alkaline water.

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The HSP/co-chaperone network in environmental cold adaptation of Chilo suppressalis

Cited by 21 publications

References 50 publications

Genome-Wide Identification and Analysis of the Heat-Shock Protein Gene Superfamily in Bemisia tabaci and Expression Pattern Analysis under Heat Shock

Genome-Wide Identification and Analysis of the Heat-Shock Protein Gene Superfamily in Bemisia tabaci and Expression Pattern Analysis under Heat Shock

Genome-wide identification and characterization of the HSP gene superfamily in apple snails (Gastropoda: Ampullariidae) and expression analysis under temperature stress

Genomic and Transcriptomic Landscape and Evolutionary Dynamics of Heat Shock Proteins in Spotted Sea Bass (Lateolabrax maculatus) under Salinity Change and Alkalinity Stress

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