GlutaredoxinV1, Main, Exploration, bibRecord, 000E94

Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin.

Identifieur interne : 000E94 ( Main/Exploration ); précédent : 000E93; suivant : 000E95

Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin.

Auteurs : Raffaele Lopreiato [Italie] ; Sonia Facchin ; Geppo Sartori ; Giorgio Arrigoni ; Stefano Casonato ; Maria Ruzzene ; Lorenzo A. Pinna ; Giovanna Carignani

Source :

The Biochemical journal [ 1470-8728 ] ; 2004.

RBID : pubmed:14519092

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Evolution, Molecular (MeSH), Glutaredoxins (MeSH), Metalloendopeptidases (chemistry), Metalloendopeptidases (metabolism), Molecular Sequence Data (MeSH), Oxidoreductases (MeSH), Phosphorylation (MeSH), Protein Structure, Tertiary (MeSH), Protein-Serine-Threonine Kinases (chemistry), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Protein-Serine-Threonine Kinases (physiology), Proteins (chemistry), Proteins (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Sequence Alignment (MeSH), Serine (metabolism), Two-Hybrid System Techniques (MeSH).
MESH :
- chemical , chemistry : Metalloendopeptidases, Protein-Serine-Threonine Kinases, Proteins, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Protein-Serine-Threonine Kinases.
- chemical , metabolism : Metalloendopeptidases, Protein-Serine-Threonine Kinases, Proteins, Saccharomyces cerevisiae Proteins, Serine.
- chemical , physiology : Protein-Serine-Threonine Kinases.
- chemical : Glutaredoxins, Oxidoreductases.
- enzymology : Saccharomyces cerevisiae.
- Amino Acid Sequence, Evolution, Molecular, Molecular Sequence Data, Phosphorylation, Protein Structure, Tertiary, Sequence Alignment, Two-Hybrid System Techniques.

Abstract

The Saccharomyces cerevisiae piD261/Bud32 protein and its structural homologues, which are present along the Archaea-Eukarya lineage, constitute a novel protein kinase family (the piD261 family) distantly related in sequence to the eukaryotic protein kinase superfamily. It has been demonstrated that the yeast protein displays Ser/Thr phosphotransferase activity in vitro and contains all the invariant residues of the family. This novel protein kinase appears to play an important cellular role as deletion in yeast of the gene encoding piD261/Bud32 results in the alteration of fundamental processes such as cell growth and sporulation. In this work we show that the phosphotransferase activity of Bud32 is relevant to its functionality in vivo, but is not the unique role of the protein, since mutants which have lost catalytic activity but not native conformation can partially complement the disruption of the gene encoding piD261/Bud32. A two-hybrid approach has led to the identification of several proteins interacting with Bud32; in particular a glutaredoxin (Grx4), a putative glycoprotease (Ykr038/Kae1) and proteins of the Imd (inosine monophosphate dehydrogenase) family seem most plausible interactors. We further demonstrate that Grx4 directly interacts with Bud32 and that it is phosphorylated in vitro by Bud32 at Ser-134. The functional significance of the interaction between Bud32 and the putative protease Ykr038/Kae1 is supported by its evolutionary conservation.

DOI: 10.1042/BJ20030638
PubMed: 14519092
PubMed Central: PMC1223863

Affiliations:

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

to stream Main, to step Corpus: 000F09
to stream Main, to step Curation: 000F09

Le document en format XML

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<term>Evolution, Molecular (MeSH)</term>
<term>Glutaredoxins (MeSH)</term>
<term>Metalloendopeptidases (chemistry)</term>
<term>Metalloendopeptidases (metabolism)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (chemistry)</term>
<term>Protein-Serine-Threonine Kinases (genetics)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>Protein-Serine-Threonine Kinases (physiology)</term>
<term>Proteins (chemistry)</term>
<term>Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Serine (metabolism)</term>
<term>Two-Hybrid System Techniques (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glutarédoxines (MeSH)</term>
<term>Metalloendopeptidases (composition chimique)</term>
<term>Metalloendopeptidases (métabolisme)</term>
<term>Oxidoreductases (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (composition chimique)</term>
<term>Protein-Serine-Threonine Kinases (génétique)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protein-Serine-Threonine Kinases (physiologie)</term>
<term>Protéines (composition chimique)</term>
<term>Protéines (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Sérine (métabolisme)</term>
<term>Techniques de double hybride (MeSH)</term>
<term>Évolution moléculaire (MeSH)</term>
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<term>Protein-Serine-Threonine Kinases</term>
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<term>Saccharomyces cerevisiae Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Metalloendopeptidases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Serine</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Protein-Serine-Threonine Kinases</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term>
<term>Oxidoreductases</term>
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<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines</term>
<term>Protéines de Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
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<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Sérine</term>
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<term>Evolution, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Phosphorylation</term>
<term>Protein Structure, Tertiary</term>
<term>Sequence Alignment</term>
<term>Two-Hybrid System Techniques</term>
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<term>Données de séquences moléculaires</term>
<term>Glutarédoxines</term>
<term>Oxidoreductases</term>
<term>Phosphorylation</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Techniques de double hybride</term>
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<front><div type="abstract" xml:lang="en">The Saccharomyces cerevisiae piD261/Bud32 protein and its structural homologues, which are present along the Archaea-Eukarya lineage, constitute a novel protein kinase family (the piD261 family) distantly related in sequence to the eukaryotic protein kinase superfamily. It has been demonstrated that the yeast protein displays Ser/Thr phosphotransferase activity in vitro and contains all the invariant residues of the family. This novel protein kinase appears to play an important cellular role as deletion in yeast of the gene encoding piD261/Bud32 results in the alteration of fundamental processes such as cell growth and sporulation. In this work we show that the phosphotransferase activity of Bud32 is relevant to its functionality in vivo, but is not the unique role of the protein, since mutants which have lost catalytic activity but not native conformation can partially complement the disruption of the gene encoding piD261/Bud32. A two-hybrid approach has led to the identification of several proteins interacting with Bud32; in particular a glutaredoxin (Grx4), a putative glycoprotease (Ykr038/Kae1) and proteins of the Imd (inosine monophosphate dehydrogenase) family seem most plausible interactors. We further demonstrate that Grx4 directly interacts with Bud32 and that it is phosphorylated in vitro by Bud32 at Ser-134. The functional significance of the interaction between Bud32 and the putative protease Ykr038/Kae1 is supported by its evolutionary conservation.</div>
</front>
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<ArticleTitle>Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin.</ArticleTitle>
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<Abstract><AbstractText>The Saccharomyces cerevisiae piD261/Bud32 protein and its structural homologues, which are present along the Archaea-Eukarya lineage, constitute a novel protein kinase family (the piD261 family) distantly related in sequence to the eukaryotic protein kinase superfamily. It has been demonstrated that the yeast protein displays Ser/Thr phosphotransferase activity in vitro and contains all the invariant residues of the family. This novel protein kinase appears to play an important cellular role as deletion in yeast of the gene encoding piD261/Bud32 results in the alteration of fundamental processes such as cell growth and sporulation. In this work we show that the phosphotransferase activity of Bud32 is relevant to its functionality in vivo, but is not the unique role of the protein, since mutants which have lost catalytic activity but not native conformation can partially complement the disruption of the gene encoding piD261/Bud32. A two-hybrid approach has led to the identification of several proteins interacting with Bud32; in particular a glutaredoxin (Grx4), a putative glycoprotease (Ykr038/Kae1) and proteins of the Imd (inosine monophosphate dehydrogenase) family seem most plausible interactors. We further demonstrate that Grx4 directly interacts with Bud32 and that it is phosphorylated in vitro by Bud32 at Ser-134. The functional significance of the interaction between Bud32 and the putative protease Ykr038/Kae1 is supported by its evolutionary conservation.</AbstractText>
</Abstract>
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<ForeName>Raffaele</ForeName>
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<Author ValidYN="Y"><LastName>Ruzzene</LastName>
<ForeName>Maria</ForeName>
<Initials>M</Initials>
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<Author ValidYN="Y"><LastName>Pinna</LastName>
<ForeName>Lorenzo A</ForeName>
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Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin.

Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin.

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