Processing of Ada protein by two serine endoproteases Do and So from Escherichia coli.
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.
Lee
C S
CS
Department of Zoology, College of Natural Sciences, Seoul National University, Korea.
Hahm
J K
JK
Hwang
B J
BJ
Park
K C
KC
Ha
D B
DB
Park
S D
SD
Chung
C H
CH
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*
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D008780:Methyltransferases; D012697:Serine Endopeptidases