Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation

Two phosphoproteins of 53,000 and 63,000 mol. wt detected in partially purified preparations of Mucor rouxii cAMP-dependent protein kinase submitted to phosphorylation conditions with [γ- 32 P]ATP are demonstrated to the the result of the autophosphorylation of its regulatory subunit, according to t...

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Autores principales: Rossi, Silvia Graciela, Guthmann, Marcelo, Moreno, Silvia N. J.
Publicado: 1992
Materias:
Autophosphorylation
cAMP-dependent protein kinase
Mucor rouxii
protein kinase A
cyclic amp dependent protein kinase
article
autophosphorylation
enzyme activation
mucor rouxii
nonhuman
priority journal
Adenosine Triphosphate
Antibodies
Binding Sites
Chromatography, Agarose
Enzyme Activation
Fungi
Immunoblotting
Molecular Weight
Phosphorus Radioisotopes
Phosphorylation
Protein Kinases
Support, Non-U.S. Gov't
Amylomyces rouxii
Mucor
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v4_n4_p443_Rossi
http://hdl.handle.net/20.500.12110/paper_08986568_v4_n4_p443_Rossi
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_08986568_v4_n4_p443_Rossi
record_format dspace
spelling paper:paper_08986568_v4_n4_p443_Rossi2023-06-08T15:49:27Z Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation Rossi, Silvia Graciela Guthmann, Marcelo Moreno, Silvia N. J. Autophosphorylation cAMP-dependent protein kinase Mucor rouxii protein kinase A cyclic amp dependent protein kinase article autophosphorylation enzyme activation mucor rouxii nonhuman priority journal Adenosine Triphosphate Antibodies Binding Sites Chromatography, Agarose Enzyme Activation Fungi Immunoblotting Molecular Weight Phosphorus Radioisotopes Phosphorylation Protein Kinases Support, Non-U.S. Gov't Amylomyces rouxii Mucor Two phosphoproteins of 53,000 and 63,000 mol. wt detected in partially purified preparations of Mucor rouxii cAMP-dependent protein kinase submitted to phosphorylation conditions with [γ- 32 P]ATP are demonstrated to the the result of the autophosphorylation of its regulatory subunit, according to the following criteria: (1) linearity of phosphate incorporation with enzyme sample; (2) independence of phosphate incorporation on temperature; (3) correlation of the phosphoproteins with enzymatic activity in a DEAE-Sepharose chromatography; (4) specific elution of the phosphorylated proteins from cAMP-agarose; (5) phosphorylation of the purified regulatory subunit. Antibodies specific against Mucor regulatory subunit detected an intact subunit of 72,000 mol. wt in crude extracts. Autophosphorylation of the fungal protein kinase A promotes activation of the holoenzyme by cAMP since: (1) under conditions of partial activations, increase of activity is observed when using the phosphoform of the enzyme; (2) release of free catalytic subunit from cAMP-agarose is enhanced when the holoenzyme is previously phosphorylated. © 1992. Fil:Rossi, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Guthmann, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1992 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v4_n4_p443_Rossi http://hdl.handle.net/20.500.12110/paper_08986568_v4_n4_p443_Rossi
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Autophosphorylation
cAMP-dependent protein kinase
Mucor rouxii
protein kinase A
cyclic amp dependent protein kinase
article
autophosphorylation
enzyme activation
mucor rouxii
nonhuman
priority journal
Adenosine Triphosphate
Antibodies
Binding Sites
Chromatography, Agarose
Enzyme Activation
Fungi
Immunoblotting
Molecular Weight
Phosphorus Radioisotopes
Phosphorylation
Protein Kinases
Support, Non-U.S. Gov't
Amylomyces rouxii
Mucor
spellingShingle Autophosphorylation
cAMP-dependent protein kinase
Mucor rouxii
protein kinase A
cyclic amp dependent protein kinase
article
autophosphorylation
enzyme activation
mucor rouxii
nonhuman
priority journal
Adenosine Triphosphate
Antibodies
Binding Sites
Chromatography, Agarose
Enzyme Activation
Fungi
Immunoblotting
Molecular Weight
Phosphorus Radioisotopes
Phosphorylation
Protein Kinases
Support, Non-U.S. Gov't
Amylomyces rouxii
Mucor
Rossi, Silvia Graciela
Guthmann, Marcelo
Moreno, Silvia N. J.
Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation
topic_facet Autophosphorylation
cAMP-dependent protein kinase
Mucor rouxii
protein kinase A
cyclic amp dependent protein kinase
article
autophosphorylation
enzyme activation
mucor rouxii
nonhuman
priority journal
Adenosine Triphosphate
Antibodies
Binding Sites
Chromatography, Agarose
Enzyme Activation
Fungi
Immunoblotting
Molecular Weight
Phosphorus Radioisotopes
Phosphorylation
Protein Kinases
Support, Non-U.S. Gov't
Amylomyces rouxii
Mucor
description Two phosphoproteins of 53,000 and 63,000 mol. wt detected in partially purified preparations of Mucor rouxii cAMP-dependent protein kinase submitted to phosphorylation conditions with [γ- 32 P]ATP are demonstrated to the the result of the autophosphorylation of its regulatory subunit, according to the following criteria: (1) linearity of phosphate incorporation with enzyme sample; (2) independence of phosphate incorporation on temperature; (3) correlation of the phosphoproteins with enzymatic activity in a DEAE-Sepharose chromatography; (4) specific elution of the phosphorylated proteins from cAMP-agarose; (5) phosphorylation of the purified regulatory subunit. Antibodies specific against Mucor regulatory subunit detected an intact subunit of 72,000 mol. wt in crude extracts. Autophosphorylation of the fungal protein kinase A promotes activation of the holoenzyme by cAMP since: (1) under conditions of partial activations, increase of activity is observed when using the phosphoform of the enzyme; (2) release of free catalytic subunit from cAMP-agarose is enhanced when the holoenzyme is previously phosphorylated. © 1992.
author Rossi, Silvia Graciela
Guthmann, Marcelo
Moreno, Silvia N. J.
author_facet Rossi, Silvia Graciela
Guthmann, Marcelo
Moreno, Silvia N. J.
author_sort Rossi, Silvia Graciela
title Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation
title_short Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation
title_full Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation
title_fullStr Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation
title_full_unstemmed Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activation
title_sort autophosphorylation of mucor rouxii camp-dependent protein kinase and its role in holoenzyme activation
publishDate 1992
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08986568_v4_n4_p443_Rossi
http://hdl.handle.net/20.500.12110/paper_08986568_v4_n4_p443_Rossi
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AT guthmannmarcelo autophosphorylationofmucorrouxiicampdependentproteinkinaseanditsroleinholoenzymeactivation
AT morenosilvianj autophosphorylationofmucorrouxiicampdependentproteinkinaseanditsroleinholoenzymeactivation
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