PMID:2159417
| Citation |
Lee, CS, Hahm, JK, Hwang, BJ, Park, KC, Ha, DB, Park, SD and Chung, CH (1990) Processing of Ada protein by two serine endoproteases Do and So from Escherichia coli. FEBS Lett. 262:310-2 |
|---|---|
| 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. |
| Links | |
| Keywords |
Bacterial Proteins/metabolism; DNA, Bacterial/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Methyltransferases/metabolism; Protein Denaturation; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism |
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