4q2s

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2s OCA], [https://pdbe.org/4q2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q2s RCSB], [https://www.ebi.ac.uk/pdbsum/4q2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2s ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

In eukaryotic cells, components of the 5' to 3' mRNA degradation machinery can undergo a rapid phase transition. The resulting cytoplasmic foci are referred to as processing bodies (P-bodies). The molecular details of the self-aggregation process are, however, largely undetermined. Herein, we use a bottom-up approach that combines NMR spectroscopy, isothermal titration calorimetry, X-ray crystallography, and fluorescence microscopy to probe if mRNA degradation factors can undergo phase transitions in vitro. We show that the Schizosaccharomyces pombe Dcp2 mRNA decapping enzyme, its prime activator Dcp1, and the scaffolding proteins Edc3 and Pdc1 are sufficient to reconstitute a phase-separation process. Intermolecular interactions between the Edc3 LSm domain and at least 10 helical leucine-rich motifs in Dcp2 and Pdc1 build the core of the interaction network. We show that blocking of these interactions interferes with the clustering behavior, both in vitro and in vivo.

In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery.,Fromm SA, Kamenz J, Noldeke ER, Neu A, Zocher G, Sprangers R Angew Chem Int Ed Engl. 2014 Jul 7;53(28):7354-9. doi: 10.1002/anie.201402885., Epub 2014 May 26. PMID:24862735<ref>PMID:24862735</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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