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CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y.
- Source :
-
Archives of biochemistry and biophysics [Arch Biochem Biophys] 2006 Jul 01; Vol. 451 (1), pp. 59-67. Date of Electronic Publication: 2006 Apr 05. - Publication Year :
- 2006
-
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.
- Subjects :
- Animals
Base Sequence
Binding Sites
Cyclic AMP-Dependent Protein Kinases metabolism
Drosophila Proteins genetics
Drosophila melanogaster
Electrophoresis, Polyacrylamide Gel
Escherichia coli genetics
Phosphoprotein Phosphatases genetics
Phosphorylation
RNA-Binding Proteins metabolism
Receptors, Neuropeptide Y genetics
Recombinant Proteins genetics
Recombinant Proteins metabolism
Surface Plasmon Resonance
Drosophila Proteins metabolism
Phosphoprotein Phosphatases metabolism
Receptors, Neuropeptide Y metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0003-9861
- Volume :
- 451
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Archives of biochemistry and biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 16631104
- Full Text :
- https://doi.org/10.1016/j.abb.2006.03.020