Purification and Properties of Factor G
This extract was created in the absence of an abstract.
Excerpt
It has been well established that in a cell-free system of E. coli two complementary factors are required for the elongation of peptide bonds on ribosomes (for recent review see Lipmann, 1969). One of them, T factor, which has been further subdivided into Tu and Ts components (Lucas-Lenard and Lipmann, 1966), catalyzes a GTP-dependent binding of aminoacyl-tRNA to ribosomes. The second factor, G factor, catalyzing a ribosome-dependent hydrolysis of GTP (Conway and Lipmann, 1964), is believed to be required for translocation of peptidyl-tRNA from aminoacyl- to peptidyl site on the ribosomes. The G factor was highly purified by Nishizuka and Lipmann (1966a) and its properties were well characterized. It has recently been crystallized by Parmeggiani (1968) and later also by Kaziro and Inoue (1968).
The studies to be reported here describe the purification and some of the properties of G factor from E. coli B, and the partial purification and...
