4B89

MIF4G domain of the yeast Not1

Summary for 4B89

• Entry DOI: 10.2210/pdb4b89/pdb
• Related: 4B8A 4B8B 4B8C
• Descriptor: GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1 (2 entities in total)
• Functional Keywords: transcription
• Biological source: SACCHAROMYCES CEREVISIAE S288C (BAKER'S YEAST)
• Cellular location: Cytoplasm: P25655
• Total number of polymer chains: 1
• Total formula weight: 28527.40

Authors

Basquin, J.,Conti, E. (deposition date: 2012-08-26, release date: 2012-11-21, Last modification date: 2024-05-01)

Primary citation

Basquin, J.,Roudko, V.V.,Rode, M.,Basquin, C.,Seraphin, B.,Conti, E.
Architecture of the Nuclease Module of the Yeast Ccr4-not Complex: The not1-Caf1-Ccr4 Interaction.
Mol.Cell, 48:207-, 2012

PubMed Abstract: Shortening eukaryotic poly(A) tails represses mRNA translation and induces mRNA turnover. The major cytoplasmic deadenylase, the Ccr4-Not complex, is a conserved multisubunit assembly. Ccr4-Not is organized around Not1, a large scaffold protein that recruits two 3'-5' exoribonucleases, Caf1 and Ccr4. We report structural studies showing that the N-terminal arm of yeast Not1 has a HEAT-repeat structure with domains related to the MIF4G fold. A MIF4G domain positioned centrally within the Not1 protein recognizes Caf1, which in turn binds the LRR domain of Ccr4 and tethers the Ccr4 nuclease domain. The interactions that form the nuclease core of the Ccr4-Not complex are evolutionarily conserved. Their specific disruption affects cell growth and mRNA deadenylation and decay in vivo in yeast. Thus, the N-terminal arm of Not1 forms an extended platform reminiscent of scaffolding proteins like eIF4G and CBP80, and places the two nucleases in a pivotal position within the Ccr4-Not complex.

PubMed: 22959269
DOI: 10.1016/J.MOLCEL.2012.08.014

Experimental method

X-RAY DIFFRACTION (1.5 Å)