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



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ID: 561654.0, MPI für Entwicklungsbiologie / Abteilung 2 - Biochemistry (E. Izaurralde)
The C-terminal alpha-alpha superhelix of Pat is required for mRNA decapping in metazoa
Authors:Braun, J. E.; Tritschler, F.; Haas, G.; Igreja, C.; Truffault, V.; Weichenrieder, O.; Izaurralde, E.
Date of Publication (YYYY-MM-DD):2010-07-21
Title of Journal:EMBO Journal
Volume:29
Issue / Number:14
Start Page:2368
End Page:2380
Review Status:not specified
Audience:Not Specified
Abstract / Description:Pat proteins regulate the transition of mRNAs from a state that is translationally active to one that is repressed, committing targeted mRNAs to degradation. Pat proteins contain a conserved N-terminal sequence, a proline-rich region, a Mid domain and a C-terminal domain (Pat-C). We show that Pat-C is essential for the interaction with mRNA decapping factors (i.e. DCP2, EDC4 and LSm1-7), whereas the P-rich region and Mid domain have distinct functions in modulating these interactions. DCP2 and EDC4 binding is enhanced by the P-rich region and does not require LSm1-7. LSm1-7 binding is assisted by the Mid domain and is reduced by the P-rich region. Structural analysis revealed that Pat-C folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain. This conserved and basic surface is required for RNA, DCP2, EDC4 and LSm1-7 binding. The multiplicity of interactions mediated by Pat-C suggests that certain of these interactions are mutually exclusive and, therefore, that Pat proteins switch decapping partners allowing transitions between sequential steps in the mRNA decapping pathway.
Free Keywords:Amino Acid Sequence; Animals; Cell Line; DNA-Binding Proteins/genetics/*metabolism; Drosophila melanogaster/genetics/metabolism; Humans; Models, Molecular; Molecular Sequence Data; Mutation; Protein Folding; *Protein Structure, Tertiary; RNA Caps/genetics/*metabolism; RNA, Messenger/genetics/*metabolism; RNA-Binding Proteins/genetics/metabolism; Recombinant Fusion Proteins/genetics/metabolism; Saccharomyces cerevisiae Proteins/genetics/metabolism; Sequence Alignment; Sequence Homology, Amino Acid
External Publication Status:published
Document Type:Article
Communicated by:root
Affiliations:MPI für Entwicklungsbiologie/Abteilung 2 - Biochemie (Elisa Izaurralde)
External Affiliations:%G eng
Identifiers:ISSN:1460-2075 (Electronic) 0261-4189 (Linking) %R embo... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/pubmed/20543818 [ID No:2]
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