TY - JOUR
T1 - Structural basis for ribosome recycling by RRF and tRNA
AU - Zhou, Dejian
AU - Tanzawa, Takehito
AU - Lin, Jinzhong
AU - Gagnon, Matthieu G.
N1 - Funding Information:
We thank M. Garcia-Blanco and H. Lander for critical reading of the manuscript and valuable suggestions. We are grateful to Y. Polikanov and M. White for their kind help and advice with the Oxford 700 series cryostream cooler. We also thank the staff of the Advanced Photon Source NE-CAT beamline 24-ID-C and of the Shanghai Synchrotron Radiation Facility beamline BL17U for help with data collection. This work was supported by grants from the National Key R&D Program of China (no. 2017YFA0504602) and the National Natural Science Foundation of China (no. 31770784) (to J.L.), and by startup funds from the University of Texas Medical Branch (to M.G.G.), by a McLaughlin Fellowship from the Institute for Human Infections and Immunity at the University of Texas Medical Branch (to M.G.G.), by a Rising Science and Technology Acquisition and Retention Program award (to M.G.G.) and by an endowment from Sealy and Smith Foundation to Sealy Center for Structural Biology at the University of Texas Medical Branch. This work is based on research conducted at the Northeastern Collaborative Access Team beamlines, which are funded by the National Institute of General Medical Sciences from the National Institutes of Health (grant no. P41-GM103403 to NE-CAT). The Pilatus 6M detector on 24-ID-C beamline is funded by the NIH–ORIP HEI Grant (no. S10-RR029205 to NE-CAT). This research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory (contract no. DE-AC02-06CH11357).
Publisher Copyright:
© 2019, The Author(s), under exclusive licence to Springer Nature America, Inc.
PY - 2020/1/1
Y1 - 2020/1/1
N2 - The bacterial ribosome is recycled into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycling factor (RRF). The molecular basis for ribosome recycling by RRF and EF-G remains unclear. Here, we report the crystal structure of a posttermination Thermus thermophilus 70S ribosome complexed with EF-G, RRF and two transfer RNAs at a resolution of 3.5 Å. The deacylated tRNA in the peptidyl (P) site moves into a previously unsuspected state of binding (peptidyl/recycling, p/R) that is analogous to that seen during initiation. The terminal end of the p/R-tRNA forms nonfavorable contacts with the 50S subunit while RRF wedges next to central inter-subunit bridges, illuminating the active roles of tRNA and RRF in dissociation of ribosomal subunits. The structure uncovers a missing snapshot of tRNA as it transits between the P and exit (E) sites, providing insights into the mechanisms of ribosome recycling and tRNA translocation.
AB - The bacterial ribosome is recycled into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycling factor (RRF). The molecular basis for ribosome recycling by RRF and EF-G remains unclear. Here, we report the crystal structure of a posttermination Thermus thermophilus 70S ribosome complexed with EF-G, RRF and two transfer RNAs at a resolution of 3.5 Å. The deacylated tRNA in the peptidyl (P) site moves into a previously unsuspected state of binding (peptidyl/recycling, p/R) that is analogous to that seen during initiation. The terminal end of the p/R-tRNA forms nonfavorable contacts with the 50S subunit while RRF wedges next to central inter-subunit bridges, illuminating the active roles of tRNA and RRF in dissociation of ribosomal subunits. The structure uncovers a missing snapshot of tRNA as it transits between the P and exit (E) sites, providing insights into the mechanisms of ribosome recycling and tRNA translocation.
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U2 - 10.1038/s41594-019-0350-7
DO - 10.1038/s41594-019-0350-7
M3 - Article
C2 - 31873307
AN - SCOPUS:85077172419
SN - 1545-9993
VL - 27
SP - 25
EP - 32
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
IS - 1
ER -