PROPERTIES OF CRYSTALLINE AMINO ACID POLYMERIZATION FACTORS FROM ESCHERICHIA COLI - BINDING OF G TO RIBOSOMES

In the past few years a great number of independent reports have indicated the requirement of the protein factors G and T for ribosomal polypeptide synthesis in the in vitro system from E. coli (1-9). With the availability of electrophoretically homogeneous, crystalline G factor (7), the importance of studying the direct interaction of this enzyme with ribosomes became evident. Moldave and co-workers already observed in the rat liver system that aminoacyltransferase II - comparable to G - binds to ribosomes in the presence of a guanine nucleotide (10, 11). In this communication, we extend our observations (12, 13) on the formation of a G-ribosome complex. © 1969.