Small heat shock proteins (HSPs) are molecular chaperones with ATP-independent properties. They are involved in a variety of physiological and stress processes. In this study, the full-length HSP 20 (HSP20) from Pinctada martensii, designated as PmHSP20, was obtained from hemocytes using rapid amplification of cDNA ends technology. The PmHSP20 cDNA was 952 bp in length, containing an open reading frame of 534 bp that encoded 177-amino acid residues, with an isoelectric point of 5.86 and molecular weight of 20.24 kDa.
Full-length cDNA of the gene checkpoint homolog 1 (Chk1) was cloned from Daphnia carinata and designated DcarChk1. DcarChk1 cDNA was 1817 bp in length and encoded a 497-amino acid polypeptide. Phylogenetic analyses revealed that DcarChk1 was most closely related to Chk1 of Daphnia pulex, followed by homologous genes of insects. Expression of DcarChk1 was higher in adult Daphnia than in larvae, and significantly higher in males than females, as determined by real-time polymerase chain reaction analysis.