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The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase

MPG-Autoren
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Schäfer,  Ingmar B.
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Rode,  Michaela
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Bonneau,  Fabien
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Schüssler,  Steffen
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Conti,  Elena
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Schäfer, I. B., Rode, M., Bonneau, F., Schüssler, S., & Conti, E. (2014). The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 21(7), 591-598. doi:10.1038/nsmb.2834.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0023-C51E-3
Zusammenfassung
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 similar to 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.