Abstract
Heat shock proteins (HSPs) consist of a large group of chaperones whose expression is induced by high temperature, hypoxia, infection and a number of other stresses. Among all the HSPs, Hsp40 is the largest HSP family, which bind to Hsp70 ATPase domain in assisting protein folding. In this study, we identified 57 hsp40s in channel catfish (Ictalurus punctatus) through in silico analysis using RNA-Seq and genome databases. These genes can be classified into three different types, Type I, II and III, based on their structural similarities. Phylogenetic and syntenic analyses provided strong evidence in supporting the orthologies of these HSPs. Meta-analyses of RNA-Seq datasets were conducted to analyze expression profile of Hsp40s following bacterial infection. Twenty seven hsp40s were found to be significantly up- or down-regulated in the liver after infection with E. ictaluri; 19 hsp40s were found to be significantly regulated in the intestine after infection with E. ictaluri; and 19 hsp40s were found to be significantly regulated in the gill following infection with F. columnare. Altogether, a total of 42 Hsp40 genes were regulated under disease situations involving three tissues and two bacterial infections. The significant regulated expression of Hsp40 genes after bacterial infection suggested their involvement in disease defenses in catfish.
Highlights
Molecular chaperones include a large and diverse group of proteins that assist in folding or unfolding of other proteins or macromolecule structures in cells [1]
heat shock proteins (HSPs) are classified based on their molecular weight to include Hsp105/110, Hsp90, Hsp70, Hsp60, Hsp40, Hsp10, and small HSPs [5]
A total of 57 Hsp40 genes were identified in channel catfish
Summary
Molecular chaperones include a large and diverse group of proteins that assist in folding or unfolding of other proteins or macromolecule structures in cells [1]. Heat shock proteins (HSPs) constitute the largest groups of chaperones. They were found to be induced under various stresses such as elevated temperature, hypoxia [2] and diseases [3, 4]. Known as DnaJ proteins, constitute one of the largest families among heat shock proteins. They regulate the ATPase activity of Hsp proteins whose function is reversibly binding to partially denatured protein substrates to avoid the aggregation of themselves or with other molecules [6,7,8]. Because the ATPase activity of Hsp70s is extremely weak, The J-domain of Hsp40s is needed for activating the ATPase domain of Hsp70s [8, 9]
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