림프구에서 특이하게 발현되는 Deubiquitinating Enzymes 의 시간별 효소활성도 = Regular Temporal Enzymatic Activity of Lymphocyte - Specific Deubiquitinating Enzymes

다국어 초록 (Multilingual Abstract)

Ubiquitin-mediated proteolysis is a rapid, highly specific molecular mechanism for regulating biological processes. This proteolysis destines proteins conjugated with ubiquitin, a small polypeptide, for either degradation by the proteasome of removal of the ubiquitin by a family of deubiquitinating enzymes, thereby stabilizing the protein form degradation. MouseDUB-1 and DUB-2 recently have been isolated and cloned. They are immediate-early genes, and are induced rapidly and transiently in response to cytokine stimuli. Since little is known regarding the mechanism of induction or substrate specificity, we have investigated the temporal enzymatic activity to understand these enzymes better. We found that both DUB-1 and DUB-2 cloned into the GST expression vector are expressed very quickly and showed the deubiquitinating enzyme activity within 30 min in response to IPTG induction. This suggests that deubiquitinating enzymes in vivo may play a role in regulating the states of ubiquitin-conjugation for protein substrates very efficiently in response to external stimuli.