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 language | English |
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Pages (from-to) | 59-67 |
Number of pages | 9 |
Journal | Archives of biochemistry and biophysics |
Volume | 451 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1 Jul 2006 |
Keywords / Materials (for Non-textual outputs)
- 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