TY - JOUR
T1 - Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon
AU - Petry, Sabine
AU - Brodersen, Ditlev E.
AU - Murphy IV, Frank V.
AU - Dunham, Christine M.
AU - Selmer, Maria
AU - Tarry, Michael J.
AU - Kelley, Ann C.
AU - Ramakrishnan, V.
N1 - Funding Information:
We thank Raimond Ravelli, Sean McSweeney, and Gordon Leonard for their help and advice at the ESRF beamlines; Garib Murshudov and Paul Adams for help and advice with the programs REFMAC and CNS, respectively; Albert Weixlbaumer and John Weir for help with synchrotron data collection; and Lori Passmore and T. Martin Schmeing for critical comments. This work was supported by the Medical Research Council (UK), NIH grant GM67624, and a grant from the Agouron Institute. S.P. is supported by a Boehringer-Ingelheim fellowship, C.M.D is supported by an American Cancer Society Postdoctoral Fellowship, and M.S. is supported by a Wenner-Gren fellowship.
PY - 2005/12/29
Y1 - 2005/12/29
N2 - During protein synthesis, translational release factors catalyze the release of the polypeptide chain when a stop codon on the mRNA reaches the A site of the ribosome. The detailed mechanism of this process is currently unknown. We present here the crystal structures of the ribosome from Thermus thermophilus with RF1 and RF2 bound to their cognate stop codons, at resolutions of 5.9 Å and 6.7 Å, respectively. The structures reveal details of interactions of the factors with the ribosome and mRNA, including elements previously implicated in decoding and peptide release. They also shed light on conformational changes both in the factors and in the ribosome during termination. Differences seen in the interaction of RF1 and RF2 with the L11 region of the ribosome allow us to rationalize previous biochemical data. Finally, this work demonstrates the feasibility of crystallizing ribosomes with bound factors at a defined state along the translational pathway.
AB - During protein synthesis, translational release factors catalyze the release of the polypeptide chain when a stop codon on the mRNA reaches the A site of the ribosome. The detailed mechanism of this process is currently unknown. We present here the crystal structures of the ribosome from Thermus thermophilus with RF1 and RF2 bound to their cognate stop codons, at resolutions of 5.9 Å and 6.7 Å, respectively. The structures reveal details of interactions of the factors with the ribosome and mRNA, including elements previously implicated in decoding and peptide release. They also shed light on conformational changes both in the factors and in the ribosome during termination. Differences seen in the interaction of RF1 and RF2 with the L11 region of the ribosome allow us to rationalize previous biochemical data. Finally, this work demonstrates the feasibility of crystallizing ribosomes with bound factors at a defined state along the translational pathway.
UR - http://www.scopus.com/inward/record.url?scp=29244487090&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=29244487090&partnerID=8YFLogxK
U2 - 10.1016/j.cell.2005.09.039
DO - 10.1016/j.cell.2005.09.039
M3 - Article
C2 - 16377566
AN - SCOPUS:29244487090
SN - 0092-8674
VL - 123
SP - 1255
EP - 1266
JO - Cell
JF - Cell
IS - 7
ER -