Cloning and analysis of DnaJ family members in the @entity12638 , XXXX .

@entity1457 @entity12638 @entity71570
UNASSIGNED: @entity1457 proteins (Hsps) are involved in a variety of critical biological functions, including protein folding, degradation, and translocation and macromolecule assembly, act as molecular chaperones during periods of stress by binding to other proteins. Using expressed sequence tag (EST) and @entity12638 ( @entity12638 ) transcriptome databases, we identified 27 cDNA sequences encoding the conserved J domain, which is found in DnaJ-type Hsps. Of the 27 J domain-containing sequences, 25 were complete cDNA sequences. We divided them into three types according to the number and presence of conserved domains. By analyzing the gene structures, intron numbers, and conserved domains and constructing a phylogenetic tree, we found that the DnaJ family had undergone convergent evolution, obtaining new domains to expand the diversity of its family members. The acquisition of the new DnaJ domains most likely occurred prior to the evolutionary divergence of prokaryotes and eukaryotes. The expression of DnaJ genes in the @entity12638 was generally higher in the fat body. The tissue distribution of @entity71570 proteins was detected by western blotting, demonstrating that in the fifth-instar larvae, the @entity71570 proteins were expressed at their highest levels in hemocytes, followed by the fat body and head. We also found that the @entity71570 transcripts were likely differentially translated in different tissues. Using immunofluorescence cytochemistry, we revealed that in the blood cells, @entity71570 was mainly localized in the cytoplasm.
