Lee J H, Kim Y S, Kim M, Baek K H
Department of Microbiology, College of Medicine, Pochon CHA University, CHA General Hospital, Seoul, Korea.
Am J Hematol. 2001 Aug;67(4):270-2. doi: 10.1002/ajh.1130.
Ubiquitin- and proteasome-mediated protein degradation is involved in many intracellular processes, including cell cycle regulation, transcriptional activation, and signal transduction in all eukaryotes. Novel subfamily members of the ubp superfamily, DUB-1 and DUB-2, are known to be immediate-early genes and are specifically expressed in B-lymphocytes and T-lymphocytes, respectively. With the site-directed mutagenesis in four conserved amino acids (Cys60, Asp133, His298, and His307) and a series of deletion in the carboxy-terminal region, we demonstrate that these conserved amino acids are critical, but not the C-terminus, for the deubiquitinating activity of DUB-2.
泛素和蛋白酶体介导的蛋白质降解参与许多细胞内过程,包括所有真核生物中的细胞周期调控、转录激活和信号转导。已知泛素特异性蛋白酶(ubp)超家族的新亚家族成员DUB-1和DUB-2是即早基因,分别在B淋巴细胞和T淋巴细胞中特异性表达。通过对四个保守氨基酸(Cys60、Asp133、His298和His307)进行定点诱变以及在羧基末端区域进行一系列缺失,我们证明这些保守氨基酸对于DUB-2的去泛素化活性至关重要,但羧基末端并非如此。