Cloning of interlukin-1 β-converting enzyme (ICE) apoptosis-related genes from Bombyx mori and its expression in Escherichia coli
ICE(interlukin-1β-converting enzyme),the first member of caspases(cys-teinylaspartate specific proteinase),plays an important role in executing of programmed cell death in multicellular organisms.In order to obtain more information about ICE of the model insect-silkworm on apoptosis pathways,ultraviolet radiation was used to stimulate silkworm cells.The total RNA of the stimulated cells was extracted and two novel isoforms of ice family were obtained by RT-PCR.They were named as ice-2 and ice-5(GenBank accession numbers:DQ360829 and DQ360830).The cDNA fragments of ice-2 and ice-5 were inserted into expression vector of pET28a.The expression of ice-2 and ice-5 in E.coli strain DE3 was induced at 37℃ and 25℃,respectively.The results showed that both the products of ice-2 and ice-5 can be modified after protein expression.