Processing of Ada protein by two serine endoproteases Do and So from Escherichia coli |
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Authors: | C S Lee J K Hahm B J Hwang K C Park D B Ha S D Park C H Chung |
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Affiliation: | Department of Zoology, College of Natural Sciences, Seoul National University, Korea. |
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Abstract: | Two soluble serine proteases Do and So from Escherichia coli were found to distinctively cleave the purified, 39 kDa Ada protein into fragments with sizes of 12-31 kDa. Protease So appears to generate a C-terminal 19 kDa polypeptide, similarly to OmpT protease. In addition, the purified 19 kDa C-terminal half of Ada protein can be further processed mainly to an 18 kDa fragment by protease So and to a 12 kDa by protease Do. These results suggest that proteases Do and So are involved in endogenous cleavage of Ada protein, which may play a role in down-regulating the adaptive response to alkylating agents. |
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