GYF domain proteomics reveals interaction sites in known and novel target proteins.

GYF domains are conserved eukaryotic adaptor domains that recognize proline-rich sequences. Although the structure and function of the prototypic GYF domain from the human CD2BP2 protein have been characterized in detail, very little is known about GYF domains from other proteins and species. Here we describe the binding properties of four GYF domains of various origins. Phage display in combination with SPOT analysis revealed the PPG(F/I/L/M/V) motif as a general recognition signature. Based on these results, the proteomes of human, yeast, and Arabidopsis thaliana were searched for potential interaction sites. Binding of several candidate proteins was confirmed by pull-down experiments or yeast two-hybrid analysis. The binding epitope of the GYF domain from the yeast SMY2 protein was mapped by NMR spectroscopy and led to a structural model that accounts for the different binding properties of SMY2-type GYF domains and the CD2BP2-GYF domain.

Citation

Michael Kofler, Kathrin Motzny, Christian Freund. GYF domain proteomics reveals interaction sites in known and novel target proteins. Molecular & cellular proteomics : MCP. 2005 Nov;4(11):1797-811

Mesh Tags

Substances

PMID: 16120600

search → result