RapamycinFungusV1, Main, Exploration, bibRecord, 001A57

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.

Identifieur interne : 001A57 ( Main/Exploration ); précédent : 001A56; suivant : 001A58

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.

Auteurs : K J Dolinski [États-Unis] ; J. Heitman

Source :

Genetics [ 0016-6731 ] ; 1999.

RBID : pubmed:10049913

Descripteurs français

KwdFr :
- Acide orotique (analogues et dérivés), Acide orotique (pharmacologie), Allèles (MeSH), Dimérisation (MeSH), Dépistage génétique (MeSH), Glucose (pharmacologie), Immunophilines (physiologie), Leucine (pharmacologie), Levures (génétique), Levures (physiologie), Modèles biologiques (MeSH), Mutagenèse (MeSH), Phénotype (MeSH), Protéines HMG (génétique), Protéines HMG (physiologie), Protéines de Saccharomyces cerevisiae (MeSH), Protéines de liaison au tacrolimus (MeSH), Protéines fongiques (génétique), Récepteurs aux peptides formylés (MeSH), Récepteurs immunologiques (génétique), Récepteurs peptidiques (génétique), Sirolimus (pharmacologie), Tacrolimus (pharmacologie), Technique de Western (MeSH), Transformation génétique (MeSH), beta-Galactosidase (génétique).
MESH :
- analogues et dérivés : Acide orotique.
- génétique : Levures, Protéines HMG, Protéines fongiques, Récepteurs immunologiques, Récepteurs peptidiques, beta-Galactosidase.
- pharmacologie : Acide orotique, Glucose, Leucine, Sirolimus, Tacrolimus.
- physiologie : Immunophilines, Levures, Protéines HMG.
- Allèles, Dimérisation, Dépistage génétique, Modèles biologiques, Mutagenèse, Phénotype, Protéines de Saccharomyces cerevisiae, Protéines de liaison au tacrolimus, Récepteurs aux peptides formylés, Technique de Western, Transformation génétique.

English descriptors

KwdEn :
- Alleles (MeSH), Blotting, Western (MeSH), Dimerization (MeSH), Fungal Proteins (genetics), Genetic Testing (MeSH), Glucose (pharmacology), High Mobility Group Proteins (genetics), High Mobility Group Proteins (physiology), Immunophilins (physiology), Leucine (pharmacology), Models, Biological (MeSH), Mutagenesis (MeSH), Orotic Acid (analogs & derivatives), Orotic Acid (pharmacology), Phenotype (MeSH), Receptors, Formyl Peptide (MeSH), Receptors, Immunologic (genetics), Receptors, Peptide (genetics), Saccharomyces cerevisiae Proteins (MeSH), Sirolimus (pharmacology), Tacrolimus (pharmacology), Tacrolimus Binding Proteins (MeSH), Transformation, Genetic (MeSH), Yeasts (genetics), Yeasts (physiology), beta-Galactosidase (genetics).
MESH :
- chemical , analogs & derivatives : Orotic Acid.
- chemical , genetics : Fungal Proteins, High Mobility Group Proteins, Receptors, Immunologic, Receptors, Peptide, beta-Galactosidase.
- chemical , pharmacology : Glucose, Leucine, Orotic Acid, Sirolimus, Tacrolimus.
- chemical , physiology : High Mobility Group Proteins, Immunophilins.
- genetics : Yeasts.
- physiology : Yeasts.
- Alleles, Blotting, Western, Dimerization, Genetic Testing, Models, Biological, Mutagenesis, Phenotype, Receptors, Formyl Peptide, Saccharomyces cerevisiae Proteins, Tacrolimus Binding Proteins, Transformation, Genetic.

Abstract

The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. FKBP12 is a ubiquitous, highly conserved, abundant enzyme that catalyzes a rate-limiting step in protein folding: peptidyl-prolyl cis-trans isomerization. However, FKBP12 is dispensible for viability in both yeast and mice, and therefore does not play an essential role in protein folding. The functions of FKBP12 may involve interactions with a number of partner proteins, and a few proteins that interact with FKBP12 in the absence of FK506 or rapamycin have been identified, including the ryanodine receptor, aspartokinase, and the type II TGF-beta receptor; however, none of these are conserved from yeast to humans. To identify other targets and functions of FKBP12, we have screened for mutations that are synthetically lethal with an FKBP12 mutation in yeast. We find that mutations in HMO1, which encodes a high mobility group 1/2 homolog, are synthetically lethal with mutations in the yeast FPR1 gene encoding FKBP12. Deltahmo1 and Deltafpr1 mutants share two phenotypes: an increased rate of plasmid loss and slow growth. In addition, Hmo1p and FKBP12 physically interact in FKBP12 affinity chromatography experiments, and two-hybrid experiments suggest that FKBP12 regulates Hmo1p-Hmo1p or Hmo1p-DNA interactions. Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions.

PubMed: 10049913
PubMed Central: PMC1460526

Affiliations:

États-Unis

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

to stream Main, to step Corpus: 001A60
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Le document en format XML

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<term>Blotting, Western (MeSH)</term>
<term>Dimerization (MeSH)</term>
<term>Fungal Proteins (genetics)</term>
<term>Genetic Testing (MeSH)</term>
<term>Glucose (pharmacology)</term>
<term>High Mobility Group Proteins (genetics)</term>
<term>High Mobility Group Proteins (physiology)</term>
<term>Immunophilins (physiology)</term>
<term>Leucine (pharmacology)</term>
<term>Models, Biological (MeSH)</term>
<term>Mutagenesis (MeSH)</term>
<term>Orotic Acid (analogs & derivatives)</term>
<term>Orotic Acid (pharmacology)</term>
<term>Phenotype (MeSH)</term>
<term>Receptors, Formyl Peptide (MeSH)</term>
<term>Receptors, Immunologic (genetics)</term>
<term>Receptors, Peptide (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (MeSH)</term>
<term>Sirolimus (pharmacology)</term>
<term>Tacrolimus (pharmacology)</term>
<term>Tacrolimus Binding Proteins (MeSH)</term>
<term>Transformation, Genetic (MeSH)</term>
<term>Yeasts (genetics)</term>
<term>Yeasts (physiology)</term>
<term>beta-Galactosidase (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acide orotique (analogues et dérivés)</term>
<term>Acide orotique (pharmacologie)</term>
<term>Allèles (MeSH)</term>
<term>Dimérisation (MeSH)</term>
<term>Dépistage génétique (MeSH)</term>
<term>Glucose (pharmacologie)</term>
<term>Immunophilines (physiologie)</term>
<term>Leucine (pharmacologie)</term>
<term>Levures (génétique)</term>
<term>Levures (physiologie)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Mutagenèse (MeSH)</term>
<term>Phénotype (MeSH)</term>
<term>Protéines HMG (génétique)</term>
<term>Protéines HMG (physiologie)</term>
<term>Protéines de Saccharomyces cerevisiae (MeSH)</term>
<term>Protéines de liaison au tacrolimus (MeSH)</term>
<term>Protéines fongiques (génétique)</term>
<term>Récepteurs aux peptides formylés (MeSH)</term>
<term>Récepteurs immunologiques (génétique)</term>
<term>Récepteurs peptidiques (génétique)</term>
<term>Sirolimus (pharmacologie)</term>
<term>Tacrolimus (pharmacologie)</term>
<term>Technique de Western (MeSH)</term>
<term>Transformation génétique (MeSH)</term>
<term>beta-Galactosidase (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Orotic Acid</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>High Mobility Group Proteins</term>
<term>Receptors, Immunologic</term>
<term>Receptors, Peptide</term>
<term>beta-Galactosidase</term>
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<term>Leucine</term>
<term>Orotic Acid</term>
<term>Sirolimus</term>
<term>Tacrolimus</term>
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<term>Immunophilins</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Yeasts</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Levures</term>
<term>Protéines HMG</term>
<term>Protéines fongiques</term>
<term>Récepteurs immunologiques</term>
<term>Récepteurs peptidiques</term>
<term>beta-Galactosidase</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide orotique</term>
<term>Glucose</term>
<term>Leucine</term>
<term>Sirolimus</term>
<term>Tacrolimus</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Immunophilines</term>
<term>Levures</term>
<term>Protéines HMG</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Yeasts</term>
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<keywords scheme="MESH" xml:lang="en"><term>Alleles</term>
<term>Blotting, Western</term>
<term>Dimerization</term>
<term>Genetic Testing</term>
<term>Models, Biological</term>
<term>Mutagenesis</term>
<term>Phenotype</term>
<term>Receptors, Formyl Peptide</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Tacrolimus Binding Proteins</term>
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<term>Dimérisation</term>
<term>Dépistage génétique</term>
<term>Modèles biologiques</term>
<term>Mutagenèse</term>
<term>Phénotype</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de liaison au tacrolimus</term>
<term>Récepteurs aux peptides formylés</term>
<term>Technique de Western</term>
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<front><div type="abstract" xml:lang="en">The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. FKBP12 is a ubiquitous, highly conserved, abundant enzyme that catalyzes a rate-limiting step in protein folding: peptidyl-prolyl cis-trans isomerization. However, FKBP12 is dispensible for viability in both yeast and mice, and therefore does not play an essential role in protein folding. The functions of FKBP12 may involve interactions with a number of partner proteins, and a few proteins that interact with FKBP12 in the absence of FK506 or rapamycin have been identified, including the ryanodine receptor, aspartokinase, and the type II TGF-beta receptor; however, none of these are conserved from yeast to humans. To identify other targets and functions of FKBP12, we have screened for mutations that are synthetically lethal with an FKBP12 mutation in yeast. We find that mutations in HMO1, which encodes a high mobility group 1/2 homolog, are synthetically lethal with mutations in the yeast FPR1 gene encoding FKBP12. Deltahmo1 and Deltafpr1 mutants share two phenotypes: an increased rate of plasmid loss and slow growth. In addition, Hmo1p and FKBP12 physically interact in FKBP12 affinity chromatography experiments, and two-hybrid experiments suggest that FKBP12 regulates Hmo1p-Hmo1p or Hmo1p-DNA interactions. Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions.</div>
</front>
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<DateCompleted><Year>1999</Year>
<Month>05</Month>
<Day>06</Day>
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<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<Title>Genetics</Title>
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<ArticleTitle>Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.</ArticleTitle>
<Pagination><MedlinePgn>935-44</MedlinePgn>
</Pagination>
<Abstract><AbstractText>The immunosuppressive drugs FK506 and rapamycin bind to the cellular protein FKBP12, and the resulting FKBP12-drug complexes inhibit signal transduction. FKBP12 is a ubiquitous, highly conserved, abundant enzyme that catalyzes a rate-limiting step in protein folding: peptidyl-prolyl cis-trans isomerization. However, FKBP12 is dispensible for viability in both yeast and mice, and therefore does not play an essential role in protein folding. The functions of FKBP12 may involve interactions with a number of partner proteins, and a few proteins that interact with FKBP12 in the absence of FK506 or rapamycin have been identified, including the ryanodine receptor, aspartokinase, and the type II TGF-beta receptor; however, none of these are conserved from yeast to humans. To identify other targets and functions of FKBP12, we have screened for mutations that are synthetically lethal with an FKBP12 mutation in yeast. We find that mutations in HMO1, which encodes a high mobility group 1/2 homolog, are synthetically lethal with mutations in the yeast FPR1 gene encoding FKBP12. Deltahmo1 and Deltafpr1 mutants share two phenotypes: an increased rate of plasmid loss and slow growth. In addition, Hmo1p and FKBP12 physically interact in FKBP12 affinity chromatography experiments, and two-hybrid experiments suggest that FKBP12 regulates Hmo1p-Hmo1p or Hmo1p-DNA interactions. Because HMG1/2 proteins are conserved from yeast to humans, our findings suggest that FKBP12-HMG1/2 interactions could represent the first conserved function of FKBP12 other than mediating FK506 and rapamycin actions.</AbstractText>
</Abstract>
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<ForeName>K J</ForeName>
<Initials>KJ</Initials>
<AffiliationInfo><Affiliation>Department of Genetics, Pharmacology and Cancer Biology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Heitman</LastName>
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<Language>eng</Language>
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<MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName>
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<MeshHeading><DescriptorName UI="D044042" MajorTopicYN="N">Receptors, Formyl Peptide</DescriptorName>
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<MeshHeading><DescriptorName UI="D011971" MajorTopicYN="N">Receptors, Immunologic</DescriptorName>
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<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="Y">Saccharomyces cerevisiae Proteins</DescriptorName>
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<MeshHeading><DescriptorName UI="D016559" MajorTopicYN="N">Tacrolimus</DescriptorName>
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.

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