title: Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation.
abstract: Messenger RNA decay, which is a regulated process intimately linked to translation, begins with the deadenylation of the poly(A) tail at the 3' end. However, the precise mechanism triggering the first step of mRNA decay and its relationship to translation have not been elucidated. Here, we show that the translation termination factor eRF3 mediates mRNA deadenylation and decay in the yeast Saccharomyces cerevisiae. The N-domain of eRF3, which is not necessarily required for translation termination, interacts with the poly(A)-binding protein PABP. When this interaction is blocked by means of deletion or overexpression of the N-domain of eRF3, half-lives of all mRNAs are prolonged. The eRF3 mutant lacking the N-domain is deficient in the poly(A) shortening. Furthermore, the eRF3-mediated mRNA decay requires translation to proceed, especially ribosomal transition through the termination codon. These results indicate that the N-domain of eRF3 mediates mRNA decay by regulating deadenylation in a manner coupled to translation.
authors.affiliation: Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Japan.
authors.forename: Nao
authors.initials: N
authors.lastname: Hosoda
authors.forename: Tetsuo
authors.initials: T
authors.lastname: Kobayashi
authors.forename: Naoyuki
authors.initials: N
authors.lastname: Uchida
authors.forename: Yuji
authors.initials: Y
authors.lastname: Funakoshi
authors.forename: Yoshiko
authors.initials: Y
authors.lastname: Kikuchi
authors.forename: Shinichi
authors.initials: S
authors.lastname: Hoshino
authors.forename: Toshiaki
authors.initials: T
authors.lastname: Katada
mesh_terms: D003062:Codon; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008957:Models, Genetic; D010454:Peptide Termination Factors / Q000378:metabolism / Q000502:physiology*; D011061:Poly A; D039102:Poly(A)-Binding Proteins / Q000378:metabolism; D011233:Precipitin Tests; D011328:Prions; D011485:Protein Binding; D014176:Protein Biosynthesis; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D013997:Time Factors
chemical_list: D003062:Codon; D005656:Fungal Proteins; D010454:Peptide Termination Factors; D039102:Poly(A)-Binding Proteins; D011328:Prions; D012333:RNA, Messenger; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C450100:pab1 protein, S cerevisiae; C087971:peptide-chain-release factor 3; D011061:Poly A; D012313:RNA