Stabilization of the Escherichia coli elongation factor Tu-GTP-aminoacyl-tRNA complex.
The effect of ammonium sulfate on the Escherichia coli elongation factor Tu-GTP-aminoacyl-tRNA complex has been studied. The half-lives of 12 E. coli aminoacyl-tRNA species were determined at 37 degrees C in the presence and absence of an equimolar amount of EF-Tu-GTP and in the presence and absence of 1.5 M ammonium sulfate. The results indicate that the addition of 1.5 M ammonium sulfate to the ternary complex increased the stability of all 12 complexes studied. In addition, the effects of various salts and crystallization agents on the stability of the E. coli EF-Tu-GTP-phenylalanyl-tRNA complex was studied in detail. Binding parameters were also measured under various conditions at 37 degrees C. The results indicate that the stability and the Kassoc of the ternary complex, using phenylalanyl-tRNA, can be increased by the presence of polyethylene glycol or ammonium sulfate.
Delaria
K
K
Department of Biochemistry, University of California, Riverside 92521.
Guillen
M
M
Louie
A
A
Jurnak
F
F
D004926:Escherichia coli / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006207:Half-Life; D007700:Kinetics; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012360:RNA, Transfer, Phe / Q000378:metabolism
D012346:RNA, Transfer, Amino Acyl; D012360:RNA, Transfer, Phe; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu