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Publication Abstract from PubMed

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-A 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-A 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.

Architecture of the ubiquitylation module of the yeast ccr4-not complex.,Bhaskar V, Basquin J, Conti E Structure. 2015 May 5;23(5):921-8. doi: 10.1016/j.str.2015.03.011. Epub 2015 Apr , 23. PMID:25914052^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.