Biochemical characterization of apoptotic cleavage of KH-type splicing regulatory protein (KSRP)/far upstream element-binding protein 2 (FBP2).
Caspases, Asp-specific cysteine protease, cleave proteins upon apoptosis. To identify and characterize new caspase substrate in the nucleus, the proteome of the rat liver extracts was analyzed after the treatment with caspases. One of the identified proteins was KSRP/FBP2 that is preferentially cleaved by caspase-3 and  7 at two sites after Asp102 and Asp183. The second site was cleaved only in the protein produced in cells, but not in in vitro translated protein. These results indicate that more than the primary sequence may be important for the recognition by caspases.
Seok
Heeyoung
H
Research Center for Proteineous Materials and Department of Bio-Materials Engineering, Chosun University, 375 Seosuk-Dong, Dong-Ku, Gwangju 501-759, Republic of Korea.
Cho
Jinsun
J
Cheon
Minseok
M
Park
Il-Seon
IS
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D053148:Caspase 3; D020169:Caspases / Q000378:metabolism; D006801:Humans; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D015534:Trans-Activators; D014407:Tumor Cells, Cultured
C105789:KHSRP protein, human; D016601:RNA-Binding Proteins; D015534:Trans-Activators; C505407:CASP3 protein, human; C505410:Casp3 protein, rat; D053148:Caspase 3; D020169:Caspases