Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that plays important roles in modulating multiple cellular stress responses. In this study, full-length complementary DNA of hsp90 from the giant spiny frog Quasipaa spinosa (Qs) was first isolated and designated as Qshsp90. This gene consisted of 2801 nucleotides with a complete open reading frame of 2172 nucleotides encoding a putative protein of 724 amino acids. Sequence analysis revealed that QsHSP90 shared high similarity with other known HSP90 and belonged to a vertebrate HSP90β subtype. Tissue distribution analysis showed that Qshsp90 was present in all of the test tissues, and its expression in liver, skin and kidney was significantly up-regulated after heat shock for 3 or 6 h, while skin showed a prompt and durable response to such heat stress. Qshsp90 transcripts in kidney and liver also markedly increased in pathogen infection models such as Aeromonas hydrophila and polyinosinic polycytidylic acid. These results indicate that Qshsp90 may play critical roles in coping mechanisms for thermal stress, and may be involved in the immune response.
- Aeromonas hydrophila
- Heat stress
- Polyinosinic polycytidylic acid
ASJC Scopus subject areas
- Aquatic Science