CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y.

TitleCG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y.
Publication TypeJournal Article
Year of Publication2006
AuthorsKókai, E., Á. Tantos, E. Vissi, B. Szöor, P. Tompa, J. Gausz, L. Alphey, P. Friedrich, and V. Dombrádi
JournalArch Biochem Biophys
Volume451
Issue1
Pagination59-67
Date Published2006 Jul 1
ISSN0003-9861
KeywordsAnimals, 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.

DOI10.1016/j.abb.2006.03.020
Alternate JournalArch. Biochem. Biophys.
PubMed ID16631104