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

doi:10.1016/j.abb.2006.03.020

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

School of Biological Sciences

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	59-67
Number of pages	9
Journal	Archives of biochemistry and biophysics
Volume	451
Issue number	1
DOIs	https://doi.org/10.1016/j.abb.2006.03.020
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

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title = "CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y",

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.",

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",

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

year = "2006",

month = jul,

day = "1",

doi = "10.1016/j.abb.2006.03.020",

language = "English",

volume = "451",

pages = "59--67",

journal = "Archives of biochemistry and biophysics",

issn = "0003-9861",

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TY - JOUR

T1 - CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y

AU - Kokai, E

AU - Tantos, A

AU - Vissi, E

AU - Szoor, B

AU - Tompa, P

AU - Gausz, J

AU - Alphey, L

AU - Friedrich, P

AU - Dombradi, Z.

PY - 2006/7/1

Y1 - 2006/7/1

N2 - 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.

AB - 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.

KW - protein phosphatases Y

KW - protein-protein interaction

KW - CG15031 gene product

KW - heat-stable unstructured RNA-binding protein

KW - Drosophila melanogaster

KW - intrinsically unstructured protein

KW - protein phosphorylation

KW - DROSOPHILA-MELANOGASTER

KW - SERINE/THREONINE PHOSPHATASE

KW - BINDING PROTEIN

KW - IDENTIFICATION

KW - SUBUNIT

KW - CLONING

KW - DISORDER

KW - LOCALIZATION

KW - PURIFICATION

KW - RECOGNITION

U2 - 10.1016/j.abb.2006.03.020

DO - 10.1016/j.abb.2006.03.020

M3 - Article

SN - 0003-9861

VL - 451

SP - 59

EP - 67

JO - Archives of biochemistry and biophysics

JF - Archives of biochemistry and biophysics

IS - 1

ER -

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

Abstract

Keywords / Materials (for Non-textual outputs)

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