RapamycinFungusV1, Main, Exploration, bibRecord, 001A87

FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.

Identifieur interne : 001A87 ( Main/Exploration ); précédent : 001A86; suivant : 001A88

FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.

Auteurs : C M Alarc N [États-Unis] ; J. Heitman

Source :

Molecular and cellular biology [ 0270-7306 ] ; 1997.

RBID : pubmed:9315655

Descripteurs français

KwdFr :
- Aspartate kinase (génétique), Aspartate kinase (métabolisme), Liaison aux protéines (MeSH), Mutation (MeSH), Protéines de fusion recombinantes (MeSH), Protéines de liaison au tacrolimus (MeSH), Protéines de liaison à l'ADN (génétique), Protéines de liaison à l'ADN (métabolisme), Protéines de transport (génétique), Protéines de transport (métabolisme), Protéines du choc thermique (génétique), Protéines du choc thermique (métabolisme), Rétroaction (MeSH), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Sites de fixation (MeSH), Tacrolimus (pharmacologie), Thréonine (analogues et dérivés), Thréonine (pharmacologie).
MESH :
- analogues et dérivés : Thréonine.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Aspartate kinase, Protéines de liaison à l'ADN, Protéines de transport, Protéines du choc thermique, Saccharomyces cerevisiae.
- métabolisme : Aspartate kinase, Protéines de liaison à l'ADN, Protéines de transport, Protéines du choc thermique.
- pharmacologie : Tacrolimus, Thréonine.
- Liaison aux protéines, Mutation, Protéines de fusion recombinantes, Protéines de liaison au tacrolimus, Rétroaction, Sites de fixation.

English descriptors

KwdEn :
- Aspartate Kinase (genetics), Aspartate Kinase (metabolism), Binding Sites (MeSH), Carrier Proteins (genetics), Carrier Proteins (metabolism), DNA-Binding Proteins (genetics), DNA-Binding Proteins (metabolism), Feedback (MeSH), Heat-Shock Proteins (genetics), Heat-Shock Proteins (metabolism), Mutation (MeSH), Protein Binding (MeSH), Recombinant Fusion Proteins (MeSH), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Tacrolimus (pharmacology), Tacrolimus Binding Proteins (MeSH), Threonine (analogs & derivatives), Threonine (pharmacology).
MESH :
- chemical , analogs & derivatives : Threonine.
- chemical , genetics : Aspartate Kinase, Carrier Proteins, DNA-Binding Proteins, Heat-Shock Proteins.
- chemical , metabolism : Aspartate Kinase, Carrier Proteins, DNA-Binding Proteins, Heat-Shock Proteins.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- chemical , pharmacology : Tacrolimus, Threonine.
- Binding Sites, Feedback, Mutation, Protein Binding, Recombinant Fusion Proteins, Tacrolimus Binding Proteins.

Abstract

The peptidyl-prolyl isomerase FKBP12 was originally identified as the intracellular receptor for the immunosuppressive drugs FK506 (tacrolimus) and rapamycin (sirolimus). Although peptidyl-prolyl isomerases have been implicated in catalyzing protein folding, the cellular functions of FKBP12 in Saccharomyces cerevisiae and other organisms are largely unknown. Using the yeast two-hybrid system, we identified aspartokinase, an enzyme that catalyzes an intermediate step in threonine and methionine biosynthesis, as an in vivo binding target of FKBP12. Aspartokinase also binds FKBP12 in vitro, and drugs that bind the FKBP12 active site, or mutations in FKBP12 surface and active site residues, disrupt the FKBP12-aspartokinase complex in vivo and in vitro.fpr1 mutants lacking FKBP12 are viable, are not threonine or methionine auxotrophs, and express wild-type levels of aspartokinase protein and activity; thus, FKBP12 is not essential for aspartokinase activity. The activity of aspartokinase is regulated by feedback inhibition by product, and genetic analyses reveal that FKBP12 is important for this feedback inhibition, possibly by catalyzing aspartokinase conformational changes in response to product binding.

DOI: 10.1128/mcb.17.10.5968
PubMed: 9315655
PubMed Central: PMC232445

Affiliations:

États-Unis

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The peptidyl-prolyl isomerase FKBP12 was originally identified as the intracellular receptor for the immunosuppressive drugs FK506 (tacrolimus) and rapamycin (sirolimus). Although peptidyl-prolyl isomerases have been implicated in catalyzing protein folding, the cellular functions of FKBP12 in Saccharomyces cerevisiae and other organisms are largely unknown. Using the yeast two-hybrid system, we identified aspartokinase, an enzyme that catalyzes an intermediate step in threonine and methionine biosynthesis, as an in vivo binding target of FKBP12. Aspartokinase also binds FKBP12 in vitro, and drugs that bind the FKBP12 active site, or mutations in FKBP12 surface and active site residues, disrupt the FKBP12-aspartokinase complex in vivo and in vitro.fpr1 mutants lacking FKBP12 are viable, are not threonine or methionine auxotrophs, and express wild-type levels of aspartokinase protein and activity; thus, FKBP12 is not essential for aspartokinase activity. The activity of aspartokinase is regulated by feedback inhibition by product, and genetic analyses reveal that FKBP12 is important for this feedback inhibition, possibly by catalyzing aspartokinase conformational changes in response to product binding.</div>
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<Abstract><AbstractText>The peptidyl-prolyl isomerase FKBP12 was originally identified as the intracellular receptor for the immunosuppressive drugs FK506 (tacrolimus) and rapamycin (sirolimus). Although peptidyl-prolyl isomerases have been implicated in catalyzing protein folding, the cellular functions of FKBP12 in Saccharomyces cerevisiae and other organisms are largely unknown. Using the yeast two-hybrid system, we identified aspartokinase, an enzyme that catalyzes an intermediate step in threonine and methionine biosynthesis, as an in vivo binding target of FKBP12. Aspartokinase also binds FKBP12 in vitro, and drugs that bind the FKBP12 active site, or mutations in FKBP12 surface and active site residues, disrupt the FKBP12-aspartokinase complex in vivo and in vitro.fpr1 mutants lacking FKBP12 are viable, are not threonine or methionine auxotrophs, and express wild-type levels of aspartokinase protein and activity; thus, FKBP12 is not essential for aspartokinase activity. The activity of aspartokinase is regulated by feedback inhibition by product, and genetic analyses reveal that FKBP12 is important for this feedback inhibition, possibly by catalyzing aspartokinase conformational changes in response to product binding.</AbstractText>
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	Serveur d'exploration sur la rapamycine et les champignons
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FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.

FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.

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