Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Int. J. Biol. Sci. (2008); 4(2):87-95 Mutation at tyrosine in AMLRY -GILRY like- motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3- Akhmaloka, Susilowati PE, Subandi, Madayanti F Biochemistry Research Division, Faculty of Mathematics, Natural Sciences, Institut Teknologi Bandung, Jln Ganesha 10, Bandung, Indonesia- loka@chem-itb-ac-id Abstract: Termination translation in Saccharomyces cerevisiae is controlled by two interacting polypeptide chain release factors, eRF1 and eRF3- Two regions in human eRF1, position at 281-305 and position at 411-415, were proposed to be involved on the interaction to eRF3- In this study we have constructed and characterized yeast eRF1 mutant at position 410 -correspond to 415 human eRF1- from tyrosine to serine residue resulting eRF1-Y410S-- The mutations did not affect the viability and temperature sensitivity of the cell- The stop codons suppression of the mutant was analyzed in vivo using PGK-stop codon-LACZ gene fusion and showed that the suppression of the mutant was significantly increased in all of codon terminations- The suppression on UAG codon was the highest increased among the stop codons by comparing the suppression of the wild type respectively- In vitro interaction between eRF1 -mutant and wild type- to eRF3 were carried out using eRF1--His-6 and eRF1-Y410S---His-6 expressed in Escherichia coli and indigenous Saccharomyces cerevisiae eRF3- The results showed that the binding affinity of eRF1-Y410S- to eRF3 was decreased up to 20% of the wild type binding affinity- Computer modeling analysis using Swiss-Prot and Amber version 9-0 programs revealed that the overall structure of eRF1-Y410S- has no significant different with the wild type- However, substitution of tyrosine to serine triggered the structural change on the other motif of C-terminal domain of eRF1- The data suggested that increasing stop codon suppression and decreasing of the binding affinity of eRF1-Y410S- were probably due to the slight modification on the structure of the C-terminal domain- [PUBMED: 18463713] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.