【摘 要】
:
The small heat shock proteins (sHSPs) are a diverse of molecular chaperones with molecular weight ranging from 12 to 43 kDa in different species.It is well
【机 构】
:
InstituteofEntomologyandMolecularBiology,ChongqingKeyLaboratoryofAnimalBiology,CollegeofLifeSciences
【出 处】
:
重庆市昆虫学会2012年学术交流及研讨会
论文部分内容阅读
The small heat shock proteins (sHSPs) are a diverse of molecular chaperones with molecular weight ranging from 12 to 43 kDa in different species.It is well established that theses proteins are crucial components of heat shock response.They also have important roles in other stress responses and in normal development.In present study,we cloned and characterized the full length cDNA of HSP23 gene from Delia antiqua,DaHSP23,by RACE PCR,quantitative real-time PCR and sequence analyses.The full-length cDNA,904 bp long,encodes 186 a.a.with a molecular mass of 20.9 kDa and a theoretical isoelectric points of 6.42.Homology analysis revealed that DaHSP23 shares more than 68% identity with known HSPs of other Diptera insects.DaHSP23 transcription is up-regulated in both summer diapauses (SD) and winter diapauses (WD) pupae with higher mRNA levels during WD than SD,while decreased when diapause was terminated.These results suggested that DaHSP23 is up-regulated in both SD and WD,and it may play an essential role in over-winterig and over-summering developmental arrest.
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