title: The C-terminal region of Ge-1 presents conserved structural features required for P-body localization.
abstract: 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.
authors.affiliation: Department of Structural Cell Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Jinek
authors.forename: Ana
authors.initials: A
authors.lastname: Eulalio
authors.forename: Andreas
authors.initials: A
authors.lastname: Lingel
authors.forename: Sigrun
authors.initials: S
authors.lastname: Helms
authors.forename: Elena
authors.initials: E
authors.lastname: Conti
authors.forename: Elisa
authors.initials: E
authors.lastname: Izaurralde