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

E Kokai, A Tantos, E Vissi, B Szoor, P Tompa, J Gausz, L Alphey, P Friedrich, Z. Dombradi

Research output: Contribution to journalArticlepeer-review

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 Escherichi a 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. (c) 2006 Elsevier Inc. All rights reserved.

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

Keywords

  • protein phosphatases Y
  • protein-protein interaction
  • CG15031 gene product
  • heat-stable unstructured RNA-binding protein
  • Drosophila melanogaster
  • intrinsically unstructured protein
  • protein phosphorylation
  • DROSOPHILA-MELANOGASTER
  • SERINE/THREONINE PHOSPHATASE
  • BINDING PROTEIN
  • IDENTIFICATION
  • SUBUNIT
  • CLONING
  • DISORDER
  • LOCALIZATION
  • PURIFICATION
  • RECOGNITION

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