Association and dissociation of the calcium-binding domains of calpain by Ca2+ |
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Authors: | Suo S Koike H Sorimachi H Ishiura S Suzuki K |
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Affiliation: | Institute of Molecular and Cellular Bioscience, University of Tokyo, Tokyo, 113-0032, Japan. |
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Abstract: | The calmodulin-like domain of calpain is important for the association of the calpain large and small subunits. We expressed the calmodulin-like domains of the large subunits of rabbit mu- and m-calpains and their small subunits in E. coli and purified them to homogeneity. Unlike the full-length subunits, the calmodulin-like domains are soluble in buffer containing Ca2+. We performed gel filtration chromatography of the purified proteins and found that all three calmodulin-like domains exist as homodimers in the absence of Ca2+ and dissociate into monomers upon the addition of Ca2+. |
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