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  Structure of a Human 4E-T/DDX6/CNOT1 Complex Reveals the Different Interplay of DDX6-Binding Proteins with the CCR4-NOT Complex

Ozgur, S., Basquin, J., Kamenska, A., Filipowicz, W., Standart, N., & Conti, E. (2015). Structure of a Human 4E-T/DDX6/CNOT1 Complex Reveals the Different Interplay of DDX6-Binding Proteins with the CCR4-NOT Complex. CELL REPORTS, 13(4), 703-711. doi:10.1016/j.celrep.2015.09.033.

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 Creators:
Ozgur, Sevim1, Author           
Basquin, Jerome1, Author           
Kamenska, Anastasiia2, Author
Filipowicz, Witold2, Author
Standart, Nancy2, 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: MESSENGER-RNA DECAY; TRANSLATIONAL REPRESSION; PROCESSING-BODIES; BINDING-PROTEIN; SACCHAROMYCES-CEREVISIAE; DEADENYLASE COMPLEXES; EIF4E-BINDING PROTEIN; CRYSTAL-STRUCTURE; DROSOPHILA CUP; CELL-LINE
 Abstract: The DEAD-box protein DDX6 is a central component of translational repression mechanisms in maternal mRNA storage in oocytes and microRNA-mediated silencing in somatic cells. DDX6 interacts with the CCR4-NOT complex and functions in concert with several post-transcriptional regulators, including Edc3, Pat1, and 4E-T. We show that the conserved CUP-homology domain (CHD) of human 4E-T interacts directly with DDX6 in both the presence and absence of the central MIF4G domain of CNOT1. The 2.1-angstrom resolution structure of the corresponding ternary complex reveals how 4E-T CHD wraps around the RecA2 domain of DDX6 and contacts CNOT1. Although 4E-T CHD lacks recognizable sequence similarity with Edc3 or Pat1, it shares the same DDX6-binding surface. In contrast to 4E-T, however, the Edc3 and Pat1 FDF motifs dissociate from DDX6 upon CNOT1 MIF4G binding in vitro. The results underscore the presence of a complex network of simultaneous and/or mutually exclusive interactions in DDX6-mediated repression.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: CELL REPORTS
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 13 (4) Sequence Number: - Start / End Page: 703 - 711 Identifier: ISSN: 2211-1247