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  Architecture of the Ubiquitylation Module of the Yeast Ccr4-Not Complex

Bhaskar, V., Basquin, J., & Conti, E. (2015). Architecture of the Ubiquitylation Module of the Yeast Ccr4-Not Complex. STRUCTURE, 23(5), 921-928. doi:10.1016/j.str.2015.03.011.

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 Creators:
Bhaskar, Varun1, Author              
Basquin, Jerome1, Author              
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: DEADENYLASE COMPLEX; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; TRANSCRIPTION FACTOR; HISTONE METHYLATION; RING-FINGER; LIGASE NOT4; E3 LIGASE; RECRUITMENT; DEGRADATION
 Abstract: The Ccr4-Not complex regulates eukaryotic gene expression at multiple levels, including mRNA turnover, translational repression, and transcription. We have studied the ubiquitylation module of the yeast Ccr4-Not complex and addressed how E3 ligase binds cognate E2 and how it is tethered to the complex. The 2.8-angstrom resolution crystal structure of the N-terminal RING domain of Not4 in complex with Ubc4 shows the detailed interactions of this E3-E2 complex. The 3.6-angstrom resolution crystal structure of the C-terminal domain of the yeast Not4 in complex with the C-terminal domain of Not1 reveals how a largely extended region at the C-terminus of Not4 wraps around a HEAT-repeat region of Not1. This C-terminal region of Not4 is only partly conserved in metazoans, rationalizing its weaker Not1-binding properties. The structural and biochemical data show how Not1 can incorporate both the ubiquitylation module and the Not2-Not3/5 module concomitantly in the Ccr4-Not complex.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000354024900016
DOI: 10.1016/j.str.2015.03.011
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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 23 (5) Sequence Number: - Start / End Page: 921 - 928 Identifier: ISSN: 0969-2126