期刊
BIOMOLECULES
卷 11, 期 10, 页码 -出版社
MDPI
DOI: 10.3390/biom11101509
关键词
molecular chaperone; heat shock protein; Hsp40; aquaculture; Streptococcosis; columnaris; RNAi
资金
- Thailand Science Research and Innovation (TSRI) [RDG6220035]
This study successfully cloned and characterized two cDNAs encoding Nile tilapia DnaJ proteins, revealing their gene structures and tissue expression patterns under normal and pathogenic infection conditions. Silencing of these genes confirmed their crucial roles in response to heat and bacterial stress, suggesting their involvement in regulating intracellular proteins during infection.
DnaJ proteins or heat shock protein 40s (HSP40s) form one of the largest heat shock protein families. In this study, 2 cDNAs encoding Nile tilapia (Oreochromis niloticus) DnaJ proteins (On-DnaJ B9b and On-DnaJ C3a) were successfully cloned and characterized. The structures and organizations of these two genes are first reported in the present study. On-DnaJ B9b is approximately 2.1 kb long and contains 2 exons and 1 intron, while On-DnaJ C3a is approximately 12 kb long and contains 12 exons and 11 introns. Under normal conditions, On-DnaJ B9b mRNA is highly expressed in gonad and trunk kidney tissues, while On-DnaJ C3a transcripts are abundantly expressed in gills, intestine, liver, and trunk kidney tissues. Following pathogenic infections, the expression of both genes is induced in the liver, spleen and head kidney tissues of Nile tilapia that were infected with two virulent pathogenic bacteria, Streptococcus agalactiae and Flavobacterium columnare. Silencing of these two genes was first carried out, and the results clearly indicated their crucial roles under both heat and bacterial stress conditions. The fundamental knowledge obtained from this study indicates the characteristic basic biofunctions of heat shock proteins in the regulation of intracellular proteins during infection, which involve preventing protein aggregation, promoting protein refolding, and activating unfolded protein degradation.
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