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

ID: 695240.0, MPI für Entwicklungsbiologie / Abteilung 2 - Biochemistry (E. Izaurralde)
Structure and assembly of the NOT module of the human CCR4-NOT complex
Authors:Boland, A.; Chen, Y.; Raisch, T.; Jonas, S.; Kuzuoglu-Ozturk, D.; Wohlbold, L.; Weichenrieder, O.; Izaurralde, E.
Date of Publication (YYYY-MM-DD):2013-11
Title of Journal:Nature Structural & Molecular Biology
Journal Abbrev.:Nat Struct Mol Biol
Issue / Number:11
Start Page:1289
End Page:1297
Sequence Number of Article:24121232
Review Status:Internal review
Audience:Experts Only
Abstract / Description:The CCR4-NOT deadenylase complex is a master regulator of translation and mRNA stability. Its NOT module orchestrates recruitment of the catalytic subunits to target mRNAs. We report the crystal structure of the human NOT module formed by the CNOT1, CNOT2 and CNOT3 C-terminal (-C) regions. CNOT1-C provides a rigid scaffold consisting of two perpendicular stacks of HEAT-like repeats. CNOT2-C and CNOT3-C heterodimerize through their SH3-like NOT-box domains. The heterodimer is stabilized and tightly anchored to the surface of CNOT1 through an unexpected intertwined arrangement of peptide regions lacking defined secondary structure. These assembly peptides mold onto their respective binding surfaces and form extensive interfaces. Mutagenesis of individual interfaces and perturbation of endogenous protein ratios cause defects in complex assembly and mRNA decay. Our studies provide a structural framework for understanding the recruitment of the CCR4-NOT complex to mRNA targets.
Free Keywords:Crystallography, X-Ray; DNA Mutational Analysis; Humans; Models, Biological; Models, Molecular; Protein Binding; Protein Conformation; Protein Multimerization; RNA, Messenger/metabolism; Receptors, CCR4/metabolism; Repressor Proteins/*chemistry/genetics/*metabolism; Transcription Factors/*chemistry/genetics/*metabolism
External Publication Status:published
Document Type:Article
Communicated by:root
Affiliations:MPI für Entwicklungsbiologie/Abteilung 2 - Biochemie (Elisa Izaurralde)
Identifiers:ISSN:1545-9985 (Electronic) 1545-9985 (Linking) %R 10.1... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/pubmed/24121232 [ID No:2]
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