Similarity, in molecular structure and function, between the plant toxin purothionin and the mammalian pore-forming proteins. |
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Authors: | T Oka Y Murata T Nakanishi H Yoshizumi H Hayashida Y Ohtsuki K Toyoshima A Hakura |
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Institution: | Department of Pathology, Kochi Medical School, Japan. |
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Abstract: | Many proteins containing domains of a cysteine-rich repeated motif, such as epidermal growth factor (EGF), have been reported. Here we report strong similarity between the amino acid sequence of a plant toxin--i.e., purothionin and its homologues--and with those of a domain found in mammalian pore-forming cytoplasmic proteins: components of complement and perforin of cytotoxic T-lymphocytes or natural killer-like cytotoxic cells. These similar sequences were found to be identical to the so-called EGF-like cysteine-rich repeated motif itself. Electron-microscopic observations indicated that, like complement and perforin, purothionin forms pores in the cytoplasmic membrane of target cells, resulting in their death within a few hours. On the basis of these sequence comparisons and physiological functions, we propose a scheme for the evolution of proteins containing modules of the cysteine-rich repeat motif. |
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