SUP45/YBR143C Literature Guide Help

Other names published for SUP45: SAL4, SUP1, SUP47, eRF1, YBR143C

SUP45 - Protein Sequence Features (23)

ReferenceOther Genes Addressed
Conard SE, et al.  (2012) Identification of eRF1 residues that play critical and complementary roles in stop codon recognition. RNA 18(6):1210-21
Helbig AO, et al.  (2010) Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels. BMC Genomics 11(1):685
Merritt GH, et al.  (2010) Decoding accuracy in eRF1 mutants and its correlation with pleiotropic quantitative traits in yeast. Nucleic Acids Res 38(16):5479-92
Hatin I, et al.  (2009) Molecular dissection of translation termination mechanism identifies two new critical regions in eRF1. Nucleic Acids Res 37(6):1789-98
Passos DO, et al.  (2009) Analysis of Dom34 and its function in no-go decay. Mol Biol Cell 20(13):3025-32
Valouev IA, et al.  (2009) Elongation factor eEF1B modulates functions of the release factors eRF1 and eRF3 and the efficiency of translation termination in yeast. BMC Mol Biol 10:60
Akhmaloka, et al.  (2008) Mutation at tyrosine in AMLRY (GILRY like) motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3. Int J Biol Sci 4(2):87-95
Amrani N, et al.  (2008) Translation factors promote the formation of two states of the closed-loop mRNP. Nature 453(7199):1276-80
Fan-Minogue H, et al.  (2008) Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination. Mol Cell 30(5):599-609
Kallmeyer AK, et al.  (2006) Eukaryotic release factor 1 phosphorylation by CK2 protein kinase is dynamic but has little effect on the efficiency of translation termination in Saccharomyces cerevisiae. Eukaryot Cell 5(8):1378-87
Salas-Marco J, et al.  (2006) Distinct paths to stop codon reassignment by the variant-code organisms Tetrahymena and Euplotes. Mol Cell Biol 26(2):438-47
Moskalenko SE, et al.  (2004) [Characterization of missense mutations in the SUP45 gene of Saccharomyces cerevisiae encoding translation termination factor eRF1] Genetika 40(5):599-606
Ito K, et al.  (2002) Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1. Proc Natl Acad Sci U S A 99(13):8494-9
Velichutina IV, et al.  (2001) Genetic interaction between yeast Saccharomyces cerevisiae release factors and the decoding region of 18 S rRNA. J Mol Biol 305(4):715-27
Bertram G, et al.  (2000) Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition. RNA 6(9):1236-47
Song H, et al.  (2000) The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100(3):311-21
Ebihara K and Nakamura Y  (1999) C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids. RNA 5(6):739-50
Eurwilaichitr L, et al.  (1999) The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol Microbiol 32(3):485-96
Ito K, et al.  (1996) Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc Natl Acad Sci U S A 93(11):5443-8
Mironova LN, et al.  (1993) [Interaction of mutations in the SUP45 (SUP1) gene in saccharomyces yeasts and their effect on protein structure] Dokl Akad Nauk 333(5):658-60
Surguchev AP and Sudarikov AB  (1987) [Analysis of the primary structure of gene sup1 and its protein product in connection with the possible evolutionary origin of the gene]. Dokl Akad Nauk SSSR 296(1):238-42
Surguchev AP, et al.  (1987) [Nucleotide sequence of a mutant allele and wild type allele SUP1 and comparison of transcripts of SUP1 and SUP2 genes] Mol Biol (Mosk) 21(2):347-58
Breining P and Piepersberg W  (1986) Yeast omnipotent supressor SUP1 (SUP45): nucleotide sequence of the wildtype and a mutant gene. Nucleic Acids Res 14(13):5187-97