Recognition and selection of tRNA in translation.
Aminoacyl-tRNA (aa-tRNA) is delivered to the ribosome in a ternary complex with elongation factor Tu (EF-Tu) and GTP. The stepwise movement of aa-tRNA from EF-Tu into the ribosomal A site entails a number of intermediates. The ribosome recognizes aa-tRNA through shape discrimination of the codon-anticodon duplex and regulates the rates of GTP hydrolysis by EF-Tu and aa-tRNA accommodation in the A site by an induced fit mechanism. Recent results of kinetic measurements, ribosome crystallography, single molecule FRET measurements, and cryo-electron microscopy suggest the mechanism of tRNA recognition and selection.
Rodnina
Marina V
MV
Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany. rodinina@uni-wh.de
Gromadski
Kirill B
KB
Kothe
Ute
U
Wieden
Hans-Joachim
HJ
D003461:Crystallography; D014176:Protein Biosynthesis / Q000502:physiology*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012270:Ribosomes / Q000737:chemistry / Q000502:physiology
D012333:RNA, Messenger; D012346:RNA, Transfer, Amino Acyl