A newly discovered function for RNase L in regulating translation termination.
The antiviral and antiproliferative effects of interferons are mediated in part by the 2'-5' oligoadenylate-RNase L RNA decay pathway. RNase L is an endoribonuclease that requires 2'-5' oligoadenylates to cleave single-stranded RNA. In this report we present evidence demonstrating a role for RNase L in translation. We identify and characterize the human translation termination factor eRF3/GSPT1 as an interacting partner of RNase L. We show that interaction of eRF3 with RNase L leads to both increased translation readthrough efficiency at premature termination codons and increased +1 frameshift efficiency at the antizyme +1 frameshift site. On the basis of our results, we present a model describing how RNase L is involved in regulating gene expression by modulating the translation termination process.
Le Roy
Florence
F
Department of Molecular Genetics, Microbiology & Immunology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
Salehzada
Tamim
T
Bisbal
Catherine
C
Dougherty
Joseph P
JP
Peltz
Stuart W
SW
D002352:Carrier Proteins / Q000378:metabolism; D045744:Cell Line, Tumor; D004722:Endoribonucleases / Q000235:genetics* / Q000378:metabolism*; D016368:Frameshift Mutation; D017930:Genes, Reporter; D006801:Humans; D008156:Luciferases / Q000235:genetics / Q000378:metabolism; D010443:Peptide Chain Termination, Translational; D010454:Peptide Termination Factors / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D016601:RNA-Binding Proteins / Q000378:metabolism
D002352:Carrier Proteins; D010454:Peptide Termination Factors; D016601:RNA-Binding Proteins; C087971:peptide-chain-release factor 3; D008156:Luciferases; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease