Expression of the pro-domain-deleted active form of caspase-6 in Escherichia coli

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Title
Expression of the pro-domain-deleted active form of caspase-6 in Escherichia coli
Author(s)
Phil Young Lee; Jin Hwa Cho; Seung-Wook ChiKwang-Hee Bae; S Cho; Byoung Chul ParkJeong Hoon KimSung Goo Park
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 24, no. 5, pp. 719-723
Publication Year
2014
Abstract
Caspases are a family of cysteine proteases that play an important role in the apoptotic pathway. Caspase-6 is an apoptosis effector that cleaves a variety of cellular substrates. The active form of the enzyme is required for use in research. However, it has been difficult to obtain sufficient quantities of active caspase-6 from Escherichia coli. In the present study, we constructed a caspase-6 with a 23-amino-acid deletion in the pro-domain. This engineered enzyme was expressed as a soluble protein in E. coli and was purified using affinity resin. In vitro enzyme assay and cleavage analysis revealed that the engineered active caspase-6 protein had characteristics similar to those of wild-type caspase-6. This novel method can be a valuable tool for obtaining active caspase-6 that can be used for screening caspase-6-specific substrates, which in turn can be used to elucidate the function of caspase-6 in apoptosis.
Keyword
Active formCaspase-6E. coliEnzyme assay
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.4014/jmb.1312.12034
Type
Article
Appears in Collections:
Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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