title: Processing of Ada protein by two serine endoproteases Do and So from Escherichia coli.
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.
authors.affiliation: Department of Zoology, College of Natural Sciences, Seoul National University, Korea.
authors.forename: C S
authors.initials: CS
authors.lastname: Lee
authors.forename: J K
authors.initials: JK
authors.lastname: Hahm
authors.forename: B J
authors.initials: BJ
authors.lastname: Hwang
authors.forename: K C
authors.initials: KC
authors.lastname: Park
authors.forename: D B
authors.initials: DB
authors.lastname: Ha
authors.forename: S D
authors.initials: SD
authors.lastname: Park
authors.forename: C H
authors.initials: CH
authors.lastname: Chung
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D004269:DNA, Bacterial / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D008780:Methyltransferases / Q000378:metabolism; D011489:Protein Denaturation; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D008780:Methyltransferases; D012697:Serine Endopeptidases