RapamycinFungusV1, Main, Exploration, bibRecord, 001A42

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo.

Identifieur interne : 001A42 ( Main/Exploration ); précédent : 001A41; suivant : 001A43

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo.

Auteurs : J. Wu [États-Unis] ; T. Tolstykh ; J. Lee ; K. Boyd ; J B Stock ; J R Broach

Source :

The EMBO journal [ 0261-4189 ] ; 2000.

RBID : pubmed:11060018

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Cattle (MeSH), Cell Cycle Proteins (chemistry), Cell Cycle Proteins (genetics), Cell Cycle Proteins (metabolism), DNA, Complementary (genetics), DNA, Complementary (isolation & purification), Drug Resistance, Microbial (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression (MeSH), Genes, Fungal (MeSH), Humans (MeSH), Methylation (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Phenotype (MeSH), Phosphoprotein Phosphatases (chemistry), Phosphoprotein Phosphatases (genetics), Phosphoprotein Phosphatases (metabolism), Protein Methyltransferases (chemistry), Protein Methyltransferases (genetics), Protein Methyltransferases (metabolism), Protein Phosphatase 2 (MeSH), Protein Subunits (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (MeSH), Schizosaccharomyces pombe Proteins (MeSH), Sequence Homology, Amino Acid (MeSH), Sirolimus (pharmacology).
MESH :
- chemical , chemistry : Cell Cycle Proteins, Fungal Proteins, Phosphoprotein Phosphatases, Protein Methyltransferases.
- chemical , genetics : Cell Cycle Proteins, DNA, Complementary, Fungal Proteins, Phosphoprotein Phosphatases, Protein Methyltransferases.
- chemical , isolation & purification : DNA, Complementary.
- chemical , metabolism : Cell Cycle Proteins, Fungal Proteins, Phosphoprotein Phosphatases, Protein Methyltransferases.
- drug effects : Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus.
- Amino Acid Sequence, Animals, Cattle, Drug Resistance, Microbial, Gene Expression, Genes, Fungal, Humans, Methylation, Molecular Sequence Data, Mutation, Phenotype, Protein Phosphatase 2, Protein Subunits, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Sequence Homology, Amino Acid.

Abstract

The phosphoprotein phosphatase 2A (PP2A) catalytic subunit contains a methyl ester on its C-terminus, which in mammalian cells is added by a specific carboxyl methyltransferase and removed by a specific carboxyl methylesterase. We have identified genes in yeast that show significant homology to human carboxyl methyltransferase and methylesterase. Extracts of wild-type yeast cells contain carboxyl methyltransferase activity, while extracts of strains deleted for one of the methyltransferase genes, PPM1, lack all activity. Mutation of PPM1 partially disrupts the PP2A holoenzyme in vivo and ppm1 mutations exhibit synthetic lethality with mutations in genes encoding the B or B' regulatory subunit. Inactivation of PPM1 or overexpression of PPE1, the yeast gene homologous to bovine methylesterase, yields phenotypes similar to those observed after inactivation of either regulatory subunit. These phenotypes can be reversed by overexpression of the B regulatory subunit. These results demonstrate that Ppm1 is the sole PP2A methyltransferase in yeast and that its activity is required for the integrity of the PP2A holoenzyme.

DOI: 10.1093/emboj/19.21.5672
PubMed: 11060018
PubMed Central: PMC305778

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Animals (MeSH)</term>
<term>Cattle (MeSH)</term>
<term>Cell Cycle Proteins (chemistry)</term>
<term>Cell Cycle Proteins (genetics)</term>
<term>Cell Cycle Proteins (metabolism)</term>
<term>DNA, Complementary (genetics)</term>
<term>DNA, Complementary (isolation & purification)</term>
<term>Drug Resistance, Microbial (MeSH)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Expression (MeSH)</term>
<term>Genes, Fungal (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Methylation (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Phenotype (MeSH)</term>
<term>Phosphoprotein Phosphatases (chemistry)</term>
<term>Phosphoprotein Phosphatases (genetics)</term>
<term>Phosphoprotein Phosphatases (metabolism)</term>
<term>Protein Methyltransferases (chemistry)</term>
<term>Protein Methyltransferases (genetics)</term>
<term>Protein Methyltransferases (metabolism)</term>
<term>Protein Phosphatase 2 (MeSH)</term>
<term>Protein Subunits (MeSH)</term>
<term>Saccharomyces cerevisiae (drug effects)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (MeSH)</term>
<term>Schizosaccharomyces pombe Proteins (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Sirolimus (pharmacology)</term>
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<term>ADN complémentaire (isolement et purification)</term>
<term>Animaux (MeSH)</term>
<term>Bovins (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Expression des gènes (MeSH)</term>
<term>Gènes fongiques (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Méthylation (MeSH)</term>
<term>Phosphoprotein Phosphatases (composition chimique)</term>
<term>Phosphoprotein Phosphatases (génétique)</term>
<term>Phosphoprotein Phosphatases (métabolisme)</term>
<term>Phénotype (MeSH)</term>
<term>Protein Methyltransferases (composition chimique)</term>
<term>Protein Methyltransferases (génétique)</term>
<term>Protein Methyltransferases (métabolisme)</term>
<term>Protein Phosphatase 2 (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (MeSH)</term>
<term>Protéines de Schizosaccharomyces pombe (MeSH)</term>
<term>Protéines du cycle cellulaire (composition chimique)</term>
<term>Protéines du cycle cellulaire (génétique)</term>
<term>Protéines du cycle cellulaire (métabolisme)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Résistance microbienne aux médicaments (MeSH)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Sirolimus (pharmacologie)</term>
<term>Sous-unités de protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cell Cycle Proteins</term>
<term>Fungal Proteins</term>
<term>Phosphoprotein Phosphatases</term>
<term>Protein Methyltransferases</term>
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<term>Fungal Proteins</term>
<term>Phosphoprotein Phosphatases</term>
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<term>Protéines du cycle cellulaire</term>
<term>Protéines fongiques</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term>
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<term>Protéines fongiques</term>
<term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>ADN complémentaire</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phosphoprotein Phosphatases</term>
<term>Protein Methyltransferases</term>
<term>Protéines du cycle cellulaire</term>
<term>Protéines fongiques</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term>
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<term>Animals</term>
<term>Cattle</term>
<term>Drug Resistance, Microbial</term>
<term>Gene Expression</term>
<term>Genes, Fungal</term>
<term>Humans</term>
<term>Methylation</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
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<term>Protein Phosphatase 2</term>
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<term>Saccharomyces cerevisiae Proteins</term>
<term>Schizosaccharomyces pombe Proteins</term>
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<term>Bovins</term>
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<term>Gènes fongiques</term>
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<term>Protéines de Schizosaccharomyces pombe</term>
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<front><div type="abstract" xml:lang="en">The phosphoprotein phosphatase 2A (PP2A) catalytic subunit contains a methyl ester on its C-terminus, which in mammalian cells is added by a specific carboxyl methyltransferase and removed by a specific carboxyl methylesterase. We have identified genes in yeast that show significant homology to human carboxyl methyltransferase and methylesterase. Extracts of wild-type yeast cells contain carboxyl methyltransferase activity, while extracts of strains deleted for one of the methyltransferase genes, PPM1, lack all activity. Mutation of PPM1 partially disrupts the PP2A holoenzyme in vivo and ppm1 mutations exhibit synthetic lethality with mutations in genes encoding the B or B' regulatory subunit. Inactivation of PPM1 or overexpression of PPE1, the yeast gene homologous to bovine methylesterase, yields phenotypes similar to those observed after inactivation of either regulatory subunit. These phenotypes can be reversed by overexpression of the B regulatory subunit. These results demonstrate that Ppm1 is the sole PP2A methyltransferase in yeast and that its activity is required for the integrity of the PP2A holoenzyme.</div>
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<Abstract><AbstractText>The phosphoprotein phosphatase 2A (PP2A) catalytic subunit contains a methyl ester on its C-terminus, which in mammalian cells is added by a specific carboxyl methyltransferase and removed by a specific carboxyl methylesterase. We have identified genes in yeast that show significant homology to human carboxyl methyltransferase and methylesterase. Extracts of wild-type yeast cells contain carboxyl methyltransferase activity, while extracts of strains deleted for one of the methyltransferase genes, PPM1, lack all activity. Mutation of PPM1 partially disrupts the PP2A holoenzyme in vivo and ppm1 mutations exhibit synthetic lethality with mutations in genes encoding the B or B' regulatory subunit. Inactivation of PPM1 or overexpression of PPE1, the yeast gene homologous to bovine methylesterase, yields phenotypes similar to those observed after inactivation of either regulatory subunit. These phenotypes can be reversed by overexpression of the B regulatory subunit. These results demonstrate that Ppm1 is the sole PP2A methyltransferase in yeast and that its activity is required for the integrity of the PP2A holoenzyme.</AbstractText>
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Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo.

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo.

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