Abstract
Simple SummaryHeat shock proteins (Hsps) are ubiquitous and conserved in almost all living organisms and are involved in a wide spectrum of cellular responses against diverse environmental stresses. However, our knowledge about the coordinated Hsp co-chaperon interaction is still limited, especially in aquatic animals facing dynamic water environments. In this study, we provided the systematic analysis of 95 Hsp genes (LmHsps) in spotted sea bass (Lateolabrax maculatus), an important aquaculture species in China, under salinity change and alkalinity stress through in silico analysis. The coordinated expression of LmHsps in response to salinity change and alkalinity stress in the gills was determined. Our results confirmed the diverse regulated expression of Hsps in L. maculatus, and that the responses to alkalinity stress may have arisen through the adaptive recruitment of LmHsp40-70-90 co-chaperons. Our results provide vital insights into the function and adaptation of aquatic animal Hsps in response to salinity-alkalinity stress.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.
Highlights
Heat shock proteins (Hsps) are highly conserved stress proteins existing broadly from prokaryotes to mammals with chaperone activity [1,2], which play essential roles in maintaining the stability of cell structure and mitigating the effect of protein misfolding and aggregation in almost all aspects of protein metabolism [3]
SHsps can bind a large range of non-native substrate proteins to form a sHsp substrate complex prior to irreversible aggregation, which becomes the target of ATP-dependent Hsp70–Hsp100 disaggregation activity [5]
To identify LmHsp genes, the coding sequences and amino acid sequences of L. maculatus genome (PRJNA408177) were blast searched using available Hsp cds and aa sequences from nine fish species, including zebrafish (Danio rerio), channel catfish (Ictalurus punetaus), stickleback (Gasterosteus aculeatus), medaka (Oryzias latipes), tilapia (Oreochromis niloticus), turbot (Scophthalmus maximus), fugu (Takifugu rubripes), Asian sea bass (Lates calcarifer), spotted gar (Lepisosteus oculatus), and four tetrapod species, including human (Homo sapiens), mouse (Mus musculus), chicken (Gallus gallus), and Xenopus (Xenopus tropicalis) from Ensemble
Summary
Heat shock proteins (Hsps) are highly conserved stress proteins existing broadly from prokaryotes to mammals with chaperone activity [1,2], which play essential roles in maintaining the stability of cell structure and mitigating the effect of protein misfolding and aggregation in almost all aspects of protein metabolism [3]. SHsps can bind a large range of non-native substrate proteins to form a sHsp substrate complex prior to irreversible aggregation, which becomes the target of ATP-dependent Hsp70–Hsp100 disaggregation activity [5]. Hsp40s, known as J-domain proteins (Dnajs), have a key role in the process of transferring substrates to their Hsp partners by stimulating the ATP hydrolysis of Hsp70 [6]. Hsp70s and Hsp90s are both ATP-dependent molecular chaperones, which perform numerous functions in a wide variety of cellular processes, including the protection of proteins from stresses [8]. SHsps function independently of ATP so as to prevent the formation of large insoluble protein aggregates [11]
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