4crn | pdb_00004crn
Cryo-EM of a pretermination complex with eRF1 and eRF3
Structural highlights
Function[ERF3_YEAST] Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.[1] [2] [3] [ERF1_YEAST] Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (By similarity).[4] Publication Abstract from PubMedTermination 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 complex containing 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. Cryoelectron Microscopic Structures of Eukaryotic Translation Termination Complexes Containing eRF1-eRF3 or eRF1-ABCE1.,Preis A, Heuer A, Barrio-Garcia C, Hauser A, Eyler DE, Berninghausen O, Green R, Becker T, Beckmann R Cell Rep. 2014 Jul 10;8(1):59-65. doi: 10.1016/j.celrep.2014.04.058. Epub 2014, Jul 4. PMID:25001285[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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