4Q2S

Crystal Structure of S. pombe Pdc1 Ge1 Domain

Summary for 4Q2S

• Entry DOI: 10.2210/pdb4q2s/pdb
• Descriptor: PDC1 GE1 DOMAIN (2 entities in total)
• Functional Keywords: ge1 domain, p-body assembly, rna binding protein
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Total number of polymer chains: 1
• Total formula weight: 16241.90

Authors

Noeldeke, E.R.,Neu, A.,Zocher, G.,Sprangers, R. (deposition date: 2014-04-09, release date: 2014-10-08, Last modification date: 2024-02-28)

Primary citation

Fromm, S.A.,Kamenz, J.,Noldeke, E.R.,Neu, A.,Zocher, G.,Sprangers, R.
In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery.
Angew.Chem.Int.Ed.Engl., 53:7354-7359, 2014

PubMed Abstract: 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.

PubMed: 24862735
DOI: 10.1002/anie.201402885

Experimental method

X-RAY DIFFRACTION (1.35 Å)