Solution of the ribosome riddle: how the ribosome selects the correct aminoacyl-tRNA out of 41 similar contestants.
Three tRNA binding sites, the A, P and E sites, have been demonstrated on ribosomes of bacterial, archaebacterial and eukaryotic origin. In all these cases the first and the third site, the A and the E site, are allosterically coupled in the sense of a negative co-operativity. Therefore, the allosteric three-site model seems to be a generally valid description of the ribosomal elongation phase, where in a cycle of reactions the nascent peptide chain is prolonged by one amino acid. The molecular concept of the allosteric three-site model explains the astonishing ability of the ribosome to select the correct substrate out of a large number of very similar substrates, and it provides a framework within which the mechanisms of the elongation factors could be understood.
Nierhaus
K H
KH
Max-Planck-Institut für Molekulare Genetik, Berlin, Germany.
D000494:Allosteric Regulation; D000926:Anticodon; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D003062:Codon; D006160:Guanosine Triphosphate / Q000378:metabolism; D008954:Models, Biological; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010441:Peptide Chain Elongation, Translational; D010445:Peptide Elongation Factors / Q000378:metabolism; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000502:physiology*; D013379:Substrate Specificity
D000926:Anticodon; D001426:Bacterial Proteins; D003062:Codon; D010445:Peptide Elongation Factors; D012329:RNA, Bacterial; D012346:RNA, Transfer, Amino Acyl; D006160:Guanosine Triphosphate