Eukaryotic translation initiation factor eIF2B,the guanine nucleotide exchange factor(GEF)for eIF2,catalyzes conversion of eIF2·GDP to eIF2·GTP.Since translation initiation can only be performed with eIF2...Eukaryotic translation initiation factor eIF2B,the guanine nucleotide exchange factor(GEF)for eIF2,catalyzes conversion of eIF2·GDP to eIF2·GTP.Since translation initiation can only be performed with eIF2·GTP,malfunction of eIF2B can cause severe problem in protein biosynthesis.Many mutations of eIF2B are associated with a neurodegenerative disease named vanishing white matter(VWM)disease or childhood ataxia with central nervous system hypomyelination(CACH).展开更多
The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<...The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<sub>1</sub> but showed no inhibitory effect in reconstituted F<sub>1</sub>F<sub>0</sub>. In 1987, G. B. Cox et al. isolated a mutant of ε subunit, and two partial revertants, Their experiments showed that F<sub>1</sub>F<sub>0</sub> complex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the展开更多
文摘Eukaryotic translation initiation factor eIF2B,the guanine nucleotide exchange factor(GEF)for eIF2,catalyzes conversion of eIF2·GDP to eIF2·GTP.Since translation initiation can only be performed with eIF2·GTP,malfunction of eIF2B can cause severe problem in protein biosynthesis.Many mutations of eIF2B are associated with a neurodegenerative disease named vanishing white matter(VWM)disease or childhood ataxia with central nervous system hypomyelination(CACH).
基金Project supported by the National Natural Science Foundation of China.
文摘The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<sub>1</sub> but showed no inhibitory effect in reconstituted F<sub>1</sub>F<sub>0</sub>. In 1987, G. B. Cox et al. isolated a mutant of ε subunit, and two partial revertants, Their experiments showed that F<sub>1</sub>F<sub>0</sub> complex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the
