Title | CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y. |
Publication Type | Journal Article |
Year of Publication | 2006 |
Authors | Kókai, E., Á. Tantos, E. Vissi, B. Szöor, P. Tompa, J. Gausz, L. Alphey, P. Friedrich, and V. Dombrádi |
Journal | Arch Biochem Biophys |
Volume | 451 |
Issue | 1 |
Pagination | 59-67 |
Date Published | 2006 Jul 1 |
ISSN | 0003-9861 |
Keywords | Animals, Base Sequence, Binding Sites, Cyclic AMP-Dependent Protein Kinases, Drosophila melanogaster, Drosophila Proteins, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Phosphoprotein Phosphatases, Phosphorylation, Receptors, Neuropeptide Y, Recombinant Proteins, RNA-Binding Proteins, Surface Plasmon Resonance |
Abstract | Protein phosphatase Y (PPY) is a Drosophila testis-specific enzyme of unknown function. In a yeast two-hybrid screen we identified CG15031/PPYR1 as a PPY interacting protein. The specificity of the protein-protein interaction was proven by directed two-hybrid tests. The complex formation between PPY and PPYR1 was confirmed under in vitro and in vivo conditions by plasmon resonance spectroscopy, co-immunoprecipitation, and pull down experiments. Recombinant PPYR1 expressed in Escherichia coli is a heatstable, protease sensitive, intrinsically unstructured RNA-binding protein that migrates anomalously in SDS-polyacrylamide gel electrophoresis. It can be phosphorylated by cAMP-dependent protein kinase in vitro. PPYR1 moderately inhibits PPY activity, the inhibitory potential of the protein is slightly increased by phosphorylation. We suggest that PPYR1 may function as a scaffolding protein that targets PPY to RNA and other protein partners in Drosophila melanogaster. |
DOI | 10.1016/j.abb.2006.03.020 |
Alternate Journal | Arch. Biochem. Biophys. |
PubMed ID | 16631104 |
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