[Elongation factor EF-Ts interacts with the aminoacyl-tRNA.EF-Tu.GTP complex].
The fluorescence polarization technique has been used to study the interaction of the EF-Ts dansyl derivative with EF-Tu after nucleotide exchange and binding of the aminoacyl-tRNA to EF-Tu.GTP. It is shown that the ternary complex formation results in the increase of EF-Ts affinity to EF-Tu and EF-Ts remains bound to EF-Tu up to the GTP hydrolysis stage on the ribosome.
Kireeva
M L
ML
Bubunenko
M G
MG
Bushueva
T L
TL
D005454:Fluorescence Polarization; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006868:Hydrolysis; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D010445:Peptide Elongation Factors / Q000378:metabolism*; D014176:Protein Biosynthesis; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D013379:Substrate Specificity
D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C023512:elongation factor Ts; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu
Faktor élongatsii EF-Ts vzaimodeĭstvuet s kompleksom aminoatsil-tRNK.EF-Tu.GTP.