Complexes of tRNA and maturation enzymes: shaping up for translation.
Several significant structures of transfer ribonucleic acid (tRNA) maturation enzymes complexed with precursor tRNA or fragments thereof have been published recently, providing detailed knowledge of enzyme-tRNA recognition and catalytic strategies. In addition to reinforcing the general principles of RNA-protein interaction, the new structures highlight both the features of composite RNA recognition by multiple enzyme subunits and the pronounced RNA structural flexibility in or near the active site in all cases. These structural principles provide plausible explanations for the exquisite specificity and catalytic power of these enzymes and, in the case of evolutionary adaptation, for the ability of some enzymes to develop novel specificities.
Li
Hong
H
Department of Chemistry and Biochemistry, Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA. hongli@sb.fsu.edu
D000818:Animals; D004722:Endoribonucleases / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins / Q000502:physiology; D006801:Humans; D007438:Introns / Q000235:genetics; D012323:RNA Processing, Post-Transcriptional / Q000502:physiology*; D012343:RNA, Transfer / Q000096:biosynthesis* / Q000235:genetics
D029968:Escherichia coli Proteins; D012343:RNA, Transfer; C510958:MnmA protein, E coli; D004722:Endoribonucleases; C051012:splicing endonuclease