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

Endre Kókai, Ágnes Tantos, Emese Vissi, Balázs Szöor, Péter Tompa, János Gausz, Luke Alphey, Péter Friedrich, Viktor Dombrádi

Research output: Contribution to journalArticle

9 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)59-67
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume451
Issue number1
DOIs
Publication statusPublished - Jul 1 2006

Keywords

  • CG15031 gene product
  • Drosophila melanogaster
  • Heat-stable unstructured RNA-binding protein
  • Intrinsically unstructured protein
  • Protein phosphatases Y
  • Protein phosphorylation
  • Protein-protein interaction

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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