• Cryo-EM structure of the mammalian eukaryotic release factor eRF1-eRF3-associated termination complex. (nature.com)
  • Elongation factor eRF3 acts in an analogous manner during the termination stage, binding and delivering eRF1 to the A site. (fieldofscience.com)
  • Hbs1 is the paralogue of eRF3 and binds Dom34, itself a paralogue of eRF1. (fieldofscience.com)
  • Termination of protein synthesis in eukaryotes involves at least two polypeptide release factors (eRFs) - eRF1 and eRF3. (biomedcentral.com)
  • Domain 3 corresponds to the C-terminal part of eRF1 that is necessary for the interaction with eRF3 although there are some discrepancies in the precise localization of the region of eRF1 that interacts with eRF3 [ 19 - 22 ]. (biomedcentral.com)
  • By contrast, eukaryotes rely on an evolutionarily unrelated omnipotent release factor (eRF1) to recognize all three stop codons 2 . (nature.com)
  • This stop codon located in the A-site of the ribosome is recognized by a release factor (RF1/RF2 in prokaryotes and eRF1 in eukaryotes), which triggers release of the nascent peptide from the ribosome. (biomedcentral.com)
  • GSPT1 is a positive regulator of translational accuracy and, in a binary complex with eRF1 (MIM 600285), functions as a polypeptide chain release factor. (wikipedia.org)
  • We found that full-length eRF1 protein is present in all mutants, although in decreased amounts. (biomedcentral.com)
  • eRF1/3 and participate in an mRNA surveillance machanism called nonsense mediated decay (NMD), promoting mRNA decay in response to premature stop codons. (fieldofscience.com)
  • We have isolated five sup45-n (n from nonsense) mutations that cause nonsense substitutions in the following amino acid positions of eRF1: Y53 → UAA, E266 → UAA, L283 → UAA, L317 → UGA, E385 → UAA. (biomedcentral.com)
  • The molecular basis of eRF1 discrimination for stop codons over sense codons is not known. (nature.com)
  • Here we present cryo-electron microscopy (cryo-EM) structures at 3.5-3.8 Å resolution of mammalian ribosomal complexes containing eRF1 interacting with each of the three stop codons in the A-site. (nature.com)
  • Binding of eRF1 flips nucleotide A1825 of 18S ribosomal RNA so that it stacks on the second and third stop codon bases. (nature.com)
  • In this compacted mRNA conformation, stop codons are favoured by a hydrogen-bonding network formed between rRNA and essential eRF1 residues that constrains the identity of the bases. (nature.com)
  • Figure 4: Molecular basis of stop codon recognition by eRF1. (nature.com)
  • eRF1 is the stop codon-recognising factor, and is a structural mimic of aa-tRNA. (fieldofscience.com)
  • Figure 2: Conformation of essential eRF1 motifs. (nature.com)
  • encodes a member of the ERF (ethylene response factor) subfamily B-3 of ERF/AP2 transcription factor family (ERF1). (or.jp)
  • Alignment of the seven known eukaryotic eRF1 sequences indicates that a highly conserved motif, GFGGIGG/A is present within the region of the C-terminus, although our deletion studies suggest that it is sequences C-terminal to this region that are functionally important. (elsevierpure.com)
  • Lately, the atomic structures of the eRF1/aRF1-related Pelota proteins (Dom34p in budding yeast) had been reported (12, 13). (monossabios.com)
  • 15. Evaluation of ETF1/eRF1, mapping to 5q31, as a candidate myeloid tumor suppressor gene. (nih.gov)
  • The aRF1/eRF1 structural domain with GGQ motif, which corresponds to the CCA arm of tRNA, contacts with all three structural domains of aEF1α showing striking tRNA mimicry of aRF1/eRF1 and its GTPase-mediated catalysis for stop codon decoding. (rcsb.org)
  • 2020 ) Nucleocytoplasmic Proteomic Analysis Uncovers eRF1 and Nonsense-Mediated Decay as Modifiers of ALS/FTD C9orf72 Toxicity. (neurotree.org)
  • eRF1/3 and participate in an mRNA surveillance machanism called nonsense mediated decay (NMD), promoting mRNA decay in response to premature stop codons. (fieldofscience.com)
  • eRF1 is the stop codon-recognising factor, and is a structural mimic of aa-tRNA. (fieldofscience.com)
  • In a crossover study, 21 healthy adult dogs were randomly assigned (in groups of 7) to receive a single oral dose (20 mg/kg) of clindamycin without excipients (control) or an extended-release formulation containing clindamycin+Hydroxypropyl methylcellulose (HPMC)+poloxamer at a ratio of 1 : 0.04 : 0.5 (ERF1) or containing clindamycin+HPMC+acrylic acid polymer (AAP) at the same proportions (ERF2). (thieme-connect.com)
  • All pharmacokinetic parameters for ERF1 and ERF2 were significantly different from those of the control treatment. (thieme-connect.com)
  • GSPT1 is a positive regulator of translational accuracy and, in a binary complex with eRF1 (MIM 600285), functions as a polypeptide chain release factor. (wikipedia.org)
  • 5. While several known genes and drought stress related transcription factors such as NAC, ERF1 and WRKY were among the positively selected and differentially expressed genes there were however several unknown genes among the positively selected genes showing differential expression. (sirna-library.com)