TY - JOUR
T1 - Cryoelectron microscopic structures of eukaryotic translation termination complexes containing eRF1-eRF3 or eRF1-ABCE1
AU - Preis, Anne
AU - Heuer, Andre
AU - Barrio-Garcia, Clara
AU - Hauser, Andreas
AU - Eyler, Daniel E.
AU - Berninghausen, Otto
AU - Green, Rachel
AU - Becker, Thomas
AU - Beckmann, Roland
N1 - Funding Information:
We thank Charlotte Ungewickell for assistance with cryo-EM and Heidemarie Sieber for assistance with biochemical experiments. This work was supported by grants from the German Research Council (GRK 1721, FOR 1805, and SFB646 to R.B., and SFB646 to T.B). R.B. acknowledges support by the Center for Integrated Protein Science and the European Research Council (Advanced Grant CRYOTRANSLATION).
PY - 2014/7/10
Y1 - 2014/7/10
N2 - Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to eRF1-loaded ribosomes to stimulate peptide release and ribosomal subunit dissociation. Here, we present cryoelectron microscopic (cryo-EM) structures of a pretermination complex containing eRF1-eRF3 and a termination/prerecycling complexcontaining eRF1-ABCE1. eRF1 undergoes drastic conformational changes: its central domain harboring the catalytically important GGQ loop is either packed against eRF3 or swung toward the peptidyl transferase center when bound to ABCE1. Additionally, in complex with eRF3, the N-terminal domain of eRF1 positions the conserved NIKS motif proximal to the stop codon, supporting its suggested role in decoding, yet it appears to be delocalized in the presence of ABCE1. These results suggest that stop codon decoding and peptide release can be uncoupled during termination.
AB - Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP hydrolysis, eRF3 dissociates, and ABCE1 can bind to eRF1-loaded ribosomes to stimulate peptide release and ribosomal subunit dissociation. Here, we present cryoelectron microscopic (cryo-EM) structures of a pretermination complex containing eRF1-eRF3 and a termination/prerecycling complexcontaining eRF1-ABCE1. eRF1 undergoes drastic conformational changes: its central domain harboring the catalytically important GGQ loop is either packed against eRF3 or swung toward the peptidyl transferase center when bound to ABCE1. Additionally, in complex with eRF3, the N-terminal domain of eRF1 positions the conserved NIKS motif proximal to the stop codon, supporting its suggested role in decoding, yet it appears to be delocalized in the presence of ABCE1. These results suggest that stop codon decoding and peptide release can be uncoupled during termination.
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U2 - 10.1016/j.celrep.2014.04.058
DO - 10.1016/j.celrep.2014.04.058
M3 - Article
C2 - 25001285
AN - SCOPUS:84904434651
SN - 2211-1247
VL - 8
SP - 59
EP - 65
JO - Cell Reports
JF - Cell Reports
IS - 1
ER -