The role of aminoacyl-tRNA binding site on the factor EF-T in uncoupled GTPase reaction.
The properties of the N-tosyl-L-phenylalanyl chloromethane treated EF-T factor were studied in a ribosomal system in which splitting of GTP occurs. The action of N-tosyl-L-phenylalanyl chloromethane inhibits the binding of aminoacyl-tRNA to the EF-T factor. The binding and exchange of guanosine phosphates continued to be preserved. The inhibited factor is inactive in the GTPase reaction which depends on the participation of ribosomes and aminoacyl-tRNA. The uncoupled GTPase reaction (which is not dependent on the presence of aminoacyl-tRNA) is also sensitive to the effect of the inhibitor. The inhibition of the uncoupled GTPase is incomplete. These findings are attributed to the involvement of the aminoacyl-tRNA binding site of the EF-T factor in the uncoupled GTPase reaction.
Sedlácek
J
J
Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 16610 Prague, Czechoslovakia.
Rychlík
I
I
Jonák
J
J
D001665:Binding Sites / Q000187:drug effects; D020558:GTP Phosphohydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D006150:Guanine Nucleotides / Q000737:chemistry; D006160:Guanosine Triphosphate / Q000737:chemistry; D010445:Peptide Elongation Factors / Q000037:antagonists & inhibitors / Q000737:chemistry*; D011485:Protein Binding / Q000187:drug effects; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D012343:RNA, Transfer / Q000737:chemistry*
D006150:Guanine Nucleotides; D010445:Peptide Elongation Factors; D011500:Protein Synthesis Inhibitors; C036506:elongation factor T; D006160:Guanosine Triphosphate; D012343:RNA, Transfer; D020558:GTP Phosphohydrolases