Biochemistry

Mimicry Strikes Again

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Science  18 Feb 2000:
Vol. 287, Issue 5456, pp. 1169
DOI: 10.1126/science.287.5456.1169c

Protein biosynthesis terminates when release factors recognize the stop codons in the messenger RNA and promote hydrolysis of the bond between the nascent polypeptide chain and the ribosome-bound transfer RNA (tRNA). Song et al. have determined the crystal structure of human eukaryotic release factor (eRF1) at 2.8 angstroms and find that it looks very much like a molecule of tRNA. A conserved gly-gly-gln motif at one end is thought to help position the water molecule used for hydrolysis while the other end is proposed to recognize the stop codon, perhaps via a thr-ala-ser ‘anticodon’ along the lines of results described by Ito et al. Structural mimicry of tRNA recently was described by Selmer et al. (Reports, 17 Dec., p. 2349) for ribosome recycling factor (RRF), which promotes disassembly of the translation machinery after termination. In both cases the structural mimicry enables the proteins to bind to the same ribosomal sites as tRNA.—VV

Cell100, 311 (2000); Nature403, 680 (2000).

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