| A small molecule that induces translational readthrough of CFTR nonsense mutations by eRF1 depletion. | A small molecule that induces translational readthrough of CFTR nonsense mutations by eRF1 depletion.
Sharma J, Du M, Wong E, Mutyam V, Li Y, Chen J, Wangen J, Thrasher K, Fu L, Peng N, Tang L, Liu K, Mathew B, Bostwick RJ, Augelli-Szafran CE, Bihler H, Liang F, Mahiou J, Saltz J, Rab A, Hong J, Sorscher EJ, Mendenhall EM, Coppola CJ, Keeling KM, Green R, Mense M, Suto MJ, Rowe SM, Bedwell DM., Free PMC Article | 08/7/2021 |
| eRF1 accumulates within elaborate nuclear envelope invaginations in patient induced pluripotent stem cell (iPSC) neurons and postmortem tissue and mediates a protective shift from protein translation to nonsense-mediated decay -dependent mRNA degradation. | Nucleocytoplasmic Proteomic Analysis Uncovers eRF1 and Nonsense-Mediated Decay as Modifiers of ALS/FTD C9orf72 Toxicity.
Ortega JA, Daley EL, Kour S, Samani M, Tellez L, Smith HS, Hall EA, Esengul YT, Tsai YH, Gendron TF, Donnelly CJ, Siddique T, Savas JN, Pandey UB, Kiskinis E., Free PMC Article | 08/1/2020 |
| We show that knockdown of human XRN1, CNOT6 and ETF1 genes in HepG2 cells led to significant alteration in stability of specific mRNAs, alterations in half-life were inversely associated with transcription rates, mostly not resulting in changes in abundance | mRNA levels are buffered upon knockdown of RNA decay and translation factors via adjustment of transcription rates in human HepG2 cells.
Singh P, James RS, Mee CJ, Morozov IY., Free PMC Article | 03/28/2020 |
| Report molecular dynamics free energy calculations on termination complexes, where relative eRF1 binding free energies to different cognate and near-cognate codons are evaluated. The simulations show a high and uniform discrimination against the near-cognate codons, that differ from the cognate ones by a single nucleotide, and reveal the structural mechanisms behind the precise decoding by eRF1. | Origin of the omnipotence of eukaryotic release factor 1.
Lind C, Oliveira A, Åqvist J., Free PMC Article | 09/22/2018 |
| The GTS loop forms a switch that is key for the multiple codon recognition capability of eRF1. | Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition.
Pillay S, Li Y, Wong LE, Pervushin K., Free PMC Article | 12/17/2016 |
| New information has been presented on architecture of the eRF1 binding site on mammalian ribosome at various translation termination steps and on conformational rearrangements induced by binding of the release factors. | Chemical footprinting reveals conformational changes of 18S and 28S rRNAs at different steps of translation termination on the human ribosome.
Bulygin KN, Bartuli YS, Malygin AA, Graifer DM, Frolova LY, Karpova GG., Free PMC Article | 06/11/2016 |
| cryo-electron microscopy (cryo-EM) structures at 3.5-3.8 A resolution of ribosomal complexes containing eRF1 interacting with each of the three stop codons in the A-site | Structural basis for stop codon recognition in eukaryotes.
Brown A, Shao S, Murray J, Hegde RS, Ramakrishnan V., Free PMC Article | 09/26/2015 |
| We characterized a region of the eRF1 N-terminal domain, the P1 pocket, that we had previously shown to be involved in termination efficiency. We identified two residues, arginine 65 and lysine 109, as critical for recognition of the three stop codons. | New insights into stop codon recognition by eRF1.
Blanchet S, Rowe M, Von der Haar T, Fabret C, Demais S, Howard MJ, Namy O., Free PMC Article | 06/27/2015 |
| C4 lysyl hydroxylation of eRF1 is required for optimal translational termination | Optimal translational termination requires C4 lysyl hydroxylation of eRF1.
Feng T, Yamamoto A, Wilkins SE, Sokolova E, Yates LA, Münzel M, Singh P, Hopkinson RJ, Fischer R, Cockman ME, Shelley J, Trudgian DC, Schödel J, McCullagh JS, Ge W, Kessler BM, Gilbert RJ, Frolova LY, Alkalaeva E, Ratcliffe PJ, Schofield CJ, Coleman ML., Free PMC Article | 04/26/2014 |
| The role of the 41 invariant and conserved N-domain residues in stop codon decoding by human eRF1 was determined. | Two-step model of stop codon recognition by eukaryotic release factor eRF1.
Kryuchkova P, Grishin A, Eliseev B, Karyagina A, Frolova L, Alkalaeva E., Free PMC Article | 06/29/2013 |
| This work provides mechanistic insight into the coordination between GTP hydrolysis by eRF3 and subsequent peptide release by eRF1. | Cryo-EM structure of the mammalian eukaryotic release factor eRF1-eRF3-associated termination complex.
Taylor D, Unbehaun A, Li W, Das S, Lei J, Liao HY, Grassucci RA, Pestova TV, Frank J., Free PMC Article | 01/26/2013 |
| Authors propose that structural variability in the GTS loop may underline the switching between omnipotency and unipotency of eRF1, implying the direct access of the GTS loop to the stop codon. | Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1.
Wong LE, Li Y, Pillay S, Frolova L, Pervushin K., Free PMC Article | 10/6/2012 |
| The NMR data show that the N-domain of human eRF1 exists in two conformational states. | Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.
Polshakov VI, Eliseev BD, Birdsall B, Frolova LY., Free PMC Article | 09/15/2012 |
| Molecular modeling of eRF1 in the 80S termination complex showed that eRF1 fragments neighboring guanines and adenines of stop signals are compatible with different N domain conformations of eRF1. | Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.
Bulygin KN, Khairulina YS, Kolosov PM, Ven'yaminova AG, Graifer DM, Vorobjev YN, Frolova LY, Karpova GG., Free PMC Article | 11/26/2011 |
| By molecular modeling, the eRF1 molecule can be fitted to the A site proximal to the P-site-bound tRNA and to a stop codon in mRNA via a large conformational change to one of its three domains. | Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.
Bulygin KN, Khairulina YS, Kolosov PM, Ven'yaminova AG, Graifer DM, Vorobjev YN, Frolova LY, Kisselev LL, Karpova GG., Free PMC Article | 10/23/2010 |
| Data show that depleting eRF1 increased the Gag-Pol to Gag ratio in cells infected with replication-competent virus. | Identification of a cellular factor that modulates HIV-1 programmed ribosomal frameshifting.
Kobayashi Y, Zhuang J, Peltz S, Dougherty J., Free PMC Article | 08/30/2010 |
| Molecular dynamics simulations show that there is no structural effect on the free RF1 release factor caused by methylation of glutamine185, suggesting that its role is intimately associated with the ribosome environment. | Does glutamine methylation affect the intrinsic conformation of the universally conserved GGQ motif in ribosomal release factors?
Andér M, Aqvist J. | 01/21/2010 |
| Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes | [Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes].
Ivanova EV, Alkalaeva EZ, Birsdall B, Kolosov PM, Pol'shakov VI, Kiselev LL. | 01/21/2010 |
| codon dependence of human eRF1 binding to the mRNA-ribosome complex | Stop codons and UGG promote efficient binding of the polypeptide release factor eRF1 to the ribosomal A site.
Chavatte L, Frolova L, Laugâa P, Kisselev L, Favre A. | 01/21/2010 |
| The invariant uridine of stop codons contacts the conserved NIKSR loop in the ribosome | The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome.
Chavatte L, Seit-Nebi A, Dubovaya V, Favre A., Free PMC Article | 01/21/2010 |
| the intracellular concentration of the eukaryotic release factor 1 (eRF1) is a critical parameter influencing the efficiency of amino acid incorporation by nonsense suppression | Downregulation of eRF1 by RNA interference increases mis-acylated tRNA suppression efficiency in human cells.
Ilegems E, Pick HM, Vogel H. | 01/21/2010 |
| bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1 | Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1.
Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M. | 01/21/2010 |
| we describe a novel complex that contains the NMD factors SMG-1 and Upf1, and the translation termination release factors eRF1 and eRF3 (SURF). | Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay.
Kashima I, Yamashita A, Izumi N, Kataoka N, Morishita R, Hoshino S, Ohno M, Dreyfuss G, Ohno S., Free PMC Article | 01/21/2010 |
| Glu55 and Tyr125 residues in the N domain of eRF1 are important for eRF1's decoding function. | Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
Kolosov P, Frolova L, Seit-Nebi A, Dubovaya V, Kononenko A, Oparina N, Justesen J, Efimov A, Kisselev L., Free PMC Article | 01/21/2010 |
| Results shows eRF1 promotes GTP binding by eRF3. | Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3.
Hauryliuk V, Zavialov A, Kisselev L, Ehrenberg M. | 01/21/2010 |