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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 2 - Biochemistry (E. Izaurralde)     Display Documents



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ID: 635944.0, MPI für Entwicklungsbiologie / Abteilung 2 - Biochemistry (E. Izaurralde)
A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation
Authors:Braun, J. E.; Truffault, V.; Boland, A.; Huntzinger, E.; Chang, C. T.; Haas, G.; Weichenrieder, O.; Coles, M.; Izaurralde, E.
Date of Publication (YYYY-MM-DD):2012-12
Title of Journal:Nat Struct Mol Biol
Volume:19
Issue / Number:12
Start Page:1324
End Page:1331
Review Status:not specified
Audience:Not Specified
Abstract / Description:The removal of the mRNA 5' cap structure by the decapping enzyme DCP2 leads to rapid 5'-->3' mRNA degradation by XRN1, suggesting that the two processes are coordinated, but the coupling mechanism is unknown. DCP2 associates with the decapping activators EDC4 and DCP1. Here we show that XRN1 directly interacts with EDC4 and DCP1 in human and Drosophila melanogaster cells, respectively. In D. melanogaster cells, this interaction is mediated by the DCP1 EVH1 domain and a DCP1-binding motif (DBM) in the XRN1 C-terminal region. The NMR structure of the DCP1 EVH1 domain bound to the DBM reveals that the peptide docks at a conserved aromatic cleft, which is used by EVH1 domains to recognize proline-rich ligands. Our findings reveal a role for XRN1 in decapping and provide a molecular basis for the coupling of decapping to 5'-->3' mRNA degradation.
Free Keywords:Amino Acid Sequence; Animals; Drosophila melanogaster; Endopeptidases/chemistry/*metabolism; Exoribonucleases/chemistry/*metabolism; Humans; Microtubule-Associated Proteins/chemistry/*metabolism; Molecular Sequence Data; Proteolysis; RNA, Messenger/*metabolism; Sequence Homology, Amino Acid
External Publication Status:published
Document Type:Article
Communicated by:root
Affiliations:MPI für Entwicklungsbiologie/Abteilung 2 - Biochemie (Elisa Izaurralde)
MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
External Affiliations:%G eng
Identifiers:ISSN:1545-9985 (Electronic) 1545-9985 (Linking) %R 10.1... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/pubmed/23142987 [ID No:2]
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