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  Structural analysis of the yeast Dhh1-Pat1 complex reveals how Dhh1 engages Pat1, Edc3 and RNA in mutually exclusive interactions

Sharif, H., Ozgur, S., Sharma, K., Basquin, C., Urlaub, H., & Conti, E. (2013). Structural analysis of the yeast Dhh1-Pat1 complex reveals how Dhh1 engages Pat1, Edc3 and RNA in mutually exclusive interactions. NUCLEIC ACIDS RESEARCH, 41(17), 8377-8390. doi:10.1093/nar/gkt600.

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 Creators:
Sharif, Humayun1, Author           
Ozgur, Sevim1, Author           
Sharma, Kundan2, Author
Basquin, Claire1, Author           
Urlaub, Henning2, Author
Conti, Elena1, Author           
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1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              

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Free keywords: JUNCTION CORE COMPLEX; OPEN SOURCE SOFTWARE; MESSENGER-RNA; CRYSTAL-STRUCTURE; TRANSLATIONAL REPRESSION; DECAPPING ENZYME; P-BODIES; PROTEIN COMPLEXES; IN-VIVO; HELICASE
 Abstract: Translational repression and deadenylation of eukaryotic mRNAs result either in the sequestration of the transcripts in a nontranslatable pool or in their degradation. Removal of the 5' cap structure is a crucial step that commits deadenylated mRNAs to 5'-to-3' degradation. Pat1, Edc3 and the DEAD-box protein Dhh1 are evolutionary conserved factors known to participate in both translational repression and decapping, but their interplay is currently unclear. We report the 2.8 A resolution structure of yeast Dhh1 bound to the N-terminal domain of Pat1. The structure shows how Pat1 wraps around the C-terminal RecA domain of Dhh1, docking onto the Phe-Asp-Phe (FDF) binding site. The FDF-binding site of Dhh1 also recognizes Edc3, revealing why the binding of Pat1 and Edc3 on Dhh1 are mutually exclusive events. Using co-immunoprecipitation assays and structure-based mutants, we demonstrate that the mode of Dhh1-Pat1 recognition is conserved in humans. Pat1 and Edc3 also interfere and compete with the RNA-binding properties of Dhh1. Mapping the RNA-binding sites on Dhh1 with a crosslinking-mass spectrometry approach shows a large RNA-binding surface around the C-terminal RecA domain, including the FDF-binding pocket. The results suggest a model for how Dhh1-containing messenger ribonucleoprotein particles might be remodeled upon Pat1 and Edc3 binding.

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Language(s): eng - English
 Dates: 2013-09
 Publication Status: Issued
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000325175900039
DOI: 10.1093/nar/gkt600
 Degree: -

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Title: NUCLEIC ACIDS RESEARCH
Source Genre: Journal
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Publ. Info: GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND : OXFORD UNIV PRESS
Pages: - Volume / Issue: 41 (17) Sequence Number: - Start / End Page: 8377 - 8390 Identifier: ISSN: 0305-1048