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The C-terminal region of Ge-1 presents conserved structural features required for P-body localization.

RNA. 2008 Oct;14(10):1991-8. Epub 2008 Aug 28
Martin Jinek 1 , Ana Eulalio , Andreas Lingel , Sigrun Helms , Elena Conti , Elisa Izaurralde
Martin Jinek 1 , Ana Eulalio , Andreas Lingel , Sigrun Helms , Elena Conti , Elisa Izaurralde
+ et al

[No authors listed]

Author information
  • 1 Department of Structural Cell Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.

摘要


The removal of the 5' cap structure by the DCP1-DCP2 decapping complex irreversibly commits eukaryotic mRNAs to degradation. In human cells, the interaction between DCP1 and DCP2 is bridged by the Ge-1 protein. Ge-1 contains an N-terminal WD40-repeat domain connected by a low-complexity region to a conserved C-terminal domain. It was reported that the C-terminal domain interacts with DCP2 and mediates Ge-1 oligomerization and P-body localization. To understand the molecular basis for these functions, we determined the three-dimensional crystal structure of the most conserved region of the Drosophila melanogaster Ge-1 C-terminal domain. The region adopts an all alpha-helical fold related to ARM- and HEAT-repeat proteins. Using structure-based mutants we identified an invariant surface residue affecting P-body localization. The conservation of critical surface and structural residues suggests that the C-terminal region adopts a similar fold with conserved functions in all members of the Ge-1 protein family.