Critical regions for deubiquitinating activity of DUB-2 expressed in T-lymphocytes.
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.
Lee
J H
JH
Department of Microbiology, College of Medicine, Pochon CHA University, CHA General Hospital, Seoul, Korea.
Kim
Y S
YS
Kim
M
M
Baek
K H
KH
D020134:Catalytic Domain / Q000235:genetics; D017124:Conserved Sequence; D010450:Endopeptidases; D006133:Growth Substances / Q000235:genetics / Q000378:metabolism; D006801:Humans; D017874:Immediate-Early Proteins / Q000235:genetics* / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D017434:Protein Structure, Tertiary; D013601:T-Lymphocytes / Q000201:enzymology*
D006133:Growth Substances; D017874:Immediate-Early Proteins; C103857:Dub2 protein, mouse; D010450:Endopeptidases