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

Authors :
Kókai E
Tantos A
Vissi E
Szöor B
Tompa P
Gausz J
Alphey L
Friedrich P
Dombrádi V
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.

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