Pan2-Pan3 is a conserved complex involved in the shortening of mRNA poly(A) tails, the initial step in eukaryotic mRNA turnover. We show that recombinant Saccharomyces cerevisiae Pan2-Pan3 can deadenylate RNAs in vitro without needing the poly(A)-binding protein Pab1. The crystal structure of an active ~200-kDa core complex reveals that Pan2 and Pan3 interact with an unusual 1:2 stoichiometry imparted by the asymmetric nature of the Pan3 homodimer. An extended region of Pan2 wraps around Pan3 and provides a major anchoring point for complex assembly. A Pan2 module formed by the pseudoubiquitin-hydrolase and RNase domains latches onto the Pan3 pseudokinase with intertwined interactions that orient the deadenylase active site toward the A-binding site of the interacting Pan3. The molecular architecture of Pan2-Pan3 suggests how the nuclease and its pseudokinase regulator act in synergy to promote deadenylation.
The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase.,Schafer IB, Rode M, Bonneau F, Schussler S, Conti E Nat Struct Mol Biol. 2014 Jun 1. doi: 10.1038/nsmb.2834. PMID:24880344[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Schafer IB, Rode M, Bonneau F, Schussler S, Conti E. The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase. Nat Struct Mol Biol. 2014 Jun 1. doi: 10.1038/nsmb.2834. PMID:24880344 doi:http://dx.doi.org/10.1038/nsmb.2834
