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 Genes Cells May (2007); 12(5):639-50 The role of N-terminal domain of translational release factor eRF3 for the control of functionality and stability in S- cerevisiae- Kodama H, Ito K, Nakamura Y Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan- Abstract: Translation termination in eukaryotes is mediated by two eukaryotic release factors, eRF1 and eRF3- eRF1 recognizes all three stop codons and induces polypeptide release, while eRF3 binds to eRF1 and participates in translation termination though the regulatory role of eRF3 is still unknown- Importantly, eRF3 interacts with various proteins of distinct biological functions- Here, we investigated the effect of these binding factors on functionality and stability of eRF3 using a temperature-sensitive mutant eRF3ts, which is susceptible to factor binding to change the growth phenotype or cellular protein level- Of factors tested, Itt1 over-expression and Sla1 knockout severely impaired viability of eRF3ts cell and its protein abundance in permissive and semipermissive conditions- Sla1 over-expression reversed the phenotype- It is reported that Itt1 and Sla1 bind to the N-terminal extension domain -NED- of eRF3, unlike the other no-effect factors that bind to the C-terminal domain -CTD-- Although NED itself is dispensable, NED-less eRF3ts altered in the stability and functionality- Moreover, Itt1-induced eRF3ts lethality was significantly restored by pep4, prb1 and prc1 knockouts that are defective in vacuolar proteolysis- These findings suggest that NED functions to switch the functional mode of eRF3 depending on the nature of binding factors- [PUBMED: 17535254] 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.