Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis

A cAMP-dependent protein kinase from mycelia of Saccobolus platensis was characterized. The holoenzyme seems to be a dimer (i.e., regulatory subunit-catalytic subunit) of 78,000 Da, slightly activated by cAMP but susceptible to dissociation into its subunits by cAMP, or by kemptide and protamine, th...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Silberstein, S., Cantore, M.L., Galvagno, M.A., Passeron, S.
Formato: JOUR
Materias:
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00039861_v282_n1_p132_Silberstein
Aporte de:
id todo:paper_00039861_v282_n1_p132_Silberstein
record_format dspace
spelling todo:paper_00039861_v282_n1_p132_Silberstein2023-10-03T13:57:00Z Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis Silberstein, S. Cantore, M.L. Galvagno, M.A. Passeron, S. cyclic amp protein kinase radioisotope article fungus nonhuman priority journal Ascomycota Centrifugation, Density Gradient Chromatography, Affinity Chromatography, DEAE-Cellulose Cyclic AMP Cytosol Electrophoresis, Polyacrylamide Gel Kinetics Macromolecular Systems Molecular Weight Protein Conformation Protein Kinases Substrate Specificity Support, Non-U.S. Gov't Bovinae Eukaryota Fungi Mammalia Saccobolus A cAMP-dependent protein kinase from mycelia of Saccobolus platensis was characterized. The holoenzyme seems to be a dimer (i.e., regulatory subunit-catalytic subunit) of 78,000 Da, slightly activated by cAMP but susceptible to dissociation into its subunits by cAMP, or by kemptide and protamine, the best substrates for Saccobolus protein kinase. The regulatory subunit was purified to homogeneity by affinity chromatography. It is highly specific for cAMP and has two types of binding sites but failed to inhibit the phosphotransferase activity of the homologous or the heterologous (bovine heart) catalytic components. The activity of the catalytic subunit was completely abolished by the regulatory component of the bovine heart protein kinase as well as by a synthetic peptide corresponding to the active site of the mammalian protein kinase inhibitor. The data suggest that interaction between the subunits of the S. platensis protein kinase is different than that found in cAMP-dependent protein kinases from other sources. Similarities and differences between the Saccobolus protein kinase and enzymes from low eucaryotes and mammalian tissues are discussed. © 1990. Fil:Cantore, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Galvagno, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v282_n1_p132_Silberstein
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic cyclic amp
protein kinase
radioisotope
article
fungus
nonhuman
priority journal
Ascomycota
Centrifugation, Density Gradient
Chromatography, Affinity
Chromatography, DEAE-Cellulose
Cyclic AMP
Cytosol
Electrophoresis, Polyacrylamide Gel
Kinetics
Macromolecular Systems
Molecular Weight
Protein Conformation
Protein Kinases
Substrate Specificity
Support, Non-U.S. Gov't
Bovinae
Eukaryota
Fungi
Mammalia
Saccobolus
spellingShingle cyclic amp
protein kinase
radioisotope
article
fungus
nonhuman
priority journal
Ascomycota
Centrifugation, Density Gradient
Chromatography, Affinity
Chromatography, DEAE-Cellulose
Cyclic AMP
Cytosol
Electrophoresis, Polyacrylamide Gel
Kinetics
Macromolecular Systems
Molecular Weight
Protein Conformation
Protein Kinases
Substrate Specificity
Support, Non-U.S. Gov't
Bovinae
Eukaryota
Fungi
Mammalia
Saccobolus
Silberstein, S.
Cantore, M.L.
Galvagno, M.A.
Passeron, S.
Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis
topic_facet cyclic amp
protein kinase
radioisotope
article
fungus
nonhuman
priority journal
Ascomycota
Centrifugation, Density Gradient
Chromatography, Affinity
Chromatography, DEAE-Cellulose
Cyclic AMP
Cytosol
Electrophoresis, Polyacrylamide Gel
Kinetics
Macromolecular Systems
Molecular Weight
Protein Conformation
Protein Kinases
Substrate Specificity
Support, Non-U.S. Gov't
Bovinae
Eukaryota
Fungi
Mammalia
Saccobolus
description A cAMP-dependent protein kinase from mycelia of Saccobolus platensis was characterized. The holoenzyme seems to be a dimer (i.e., regulatory subunit-catalytic subunit) of 78,000 Da, slightly activated by cAMP but susceptible to dissociation into its subunits by cAMP, or by kemptide and protamine, the best substrates for Saccobolus protein kinase. The regulatory subunit was purified to homogeneity by affinity chromatography. It is highly specific for cAMP and has two types of binding sites but failed to inhibit the phosphotransferase activity of the homologous or the heterologous (bovine heart) catalytic components. The activity of the catalytic subunit was completely abolished by the regulatory component of the bovine heart protein kinase as well as by a synthetic peptide corresponding to the active site of the mammalian protein kinase inhibitor. The data suggest that interaction between the subunits of the S. platensis protein kinase is different than that found in cAMP-dependent protein kinases from other sources. Similarities and differences between the Saccobolus protein kinase and enzymes from low eucaryotes and mammalian tissues are discussed. © 1990.
format JOUR
author Silberstein, S.
Cantore, M.L.
Galvagno, M.A.
Passeron, S.
author_facet Silberstein, S.
Cantore, M.L.
Galvagno, M.A.
Passeron, S.
author_sort Silberstein, S.
title Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis
title_short Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis
title_full Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis
title_fullStr Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis
title_full_unstemmed Isolation and characterization of a dimeric cAMP-dependent protein kinase from the fungus Saccobolus platensis
title_sort isolation and characterization of a dimeric camp-dependent protein kinase from the fungus saccobolus platensis
url http://hdl.handle.net/20.500.12110/paper_00039861_v282_n1_p132_Silberstein
work_keys_str_mv AT silbersteins isolationandcharacterizationofadimericcampdependentproteinkinasefromthefungussaccobolusplatensis
AT cantoreml isolationandcharacterizationofadimericcampdependentproteinkinasefromthefungussaccobolusplatensis
AT galvagnoma isolationandcharacterizationofadimericcampdependentproteinkinasefromthefungussaccobolusplatensis
AT passerons isolationandcharacterizationofadimericcampdependentproteinkinasefromthefungussaccobolusplatensis
_version_ 1782028797909925888