Making sense of mimic in translation termination.
The mechanism of translation termination has long been a puzzle. Recent crystallographic evidence suggests that the eukaryotic release factor (eRF1), the bacterial release factor (RF2) and the ribosome recycling factor (RRF) all mimic a tRNA structure, whereas biochemical and genetic evidence supports the idea of a tripeptide 'anticodon' in bacterial release factors RF1 and RF2. However, the suggested structural mimicry of RF2 is not in agreement with the tripeptide 'anticodon' hypothesis and, furthermore, recently determined structures using cryo-electron microscopy show that, when bound to the ribosome, RF2 has a conformation that is distinct from the RF2 crystal structure. In addition, hydroxyl-radical probings of RRF on the ribosome are not in agreement with the simple idea that RRF mimics tRNA in the ribosome A-site. All of this evidence seriously questions the simple concept of structural mimicry between proteins and RNA and, thus, leaves only functional mimicry of protein factors of translation to be investigated.
Nakamura
Yoshikazu
Y
Department of Basic Medical Sciences, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan. nak@ims.u-tokyo.ac.jp
Ito
Koichi
K
D000926:Anticodon / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D008954:Models, Biological; D008958:Models, Molecular; D018716:Molecular Mimicry; D010454:Peptide Termination Factors / Q000737:chemistry* / Q000378:metabolism; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012343:RNA, Transfer / Q000235:genetics / Q000502:physiology*
D000926:Anticodon; D010454:Peptide Termination Factors; D012343:RNA, Transfer