Identification of a self-association domain in the Ewing's sarcoma protein: a novel function for arginine-glycine-glycine rich motifs?

DJ Shaw, R Morse, AG Todd, P Eggleton… - The journal of …, 2010 - academic.oup.com
DJ Shaw, R Morse, AG Todd, P Eggleton, CL Lorson, PJ Young
The journal of biochemistry, 2010academic.oup.com
The Ewing's sarcoma (EWS) protein is a ubiquitously expressed RNA chaperone. The EWS
protein localizes predominantly to the nucleus. Previous reports have suggested that the
EWS protein is capable of dimerizing. However, to date this has not been confirmed. Here,
using a novel panel of recombinant proteins, we have performed an in vitro biomolecular
interaction analysis of the EWS protein. We have demonstrated that all three arginine-
glycine-glycine (RGG) motifs are capable of binding directly to the survival motor neuron …
Abstract
The Ewing’s sarcoma (EWS) protein is a ubiquitously expressed RNA chaperone. The EWS protein localizes predominantly to the nucleus. Previous reports have suggested that the EWS protein is capable of dimerizing. However, to date this has not been confirmed. Here, using a novel panel of recombinant proteins, we have performed an in vitro biomolecular interaction analysis of the EWS protein. We have demonstrated that all three arginine-glycine-glycine (RGG) motifs are capable of binding directly to the survival motor neuron protein, a Tudor domain containing EWS binding partner. We have also confirmed EWS is capable of self-associating, and we have mapped this binding domain to the RGG motifs. We have also found that self-association may be required for EWS nuclear import. This is the first direct evidence of RGG domains being involved in self-association and has implications on all RGG-containing proteins.
Oxford University Press