RapamycinFungusV1, Main, Exploration, bibRecord, 001943

Domains of Gln3p interacting with karyopherins, Ure2p, and the target of rapamycin protein.

Identifieur interne : 001943 ( Main/Exploration ); précédent : 001942; suivant : 001944

Domains of Gln3p interacting with karyopherins, Ure2p, and the target of rapamycin protein.

Auteurs : John Carvalho [États-Unis] ; X F Steven Zheng

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2003.

RBID : pubmed:12624103

Descripteurs français

KwdFr :
- Caryophérines (métabolisme), Facteurs de transcription (analyse), Facteurs de transcription (métabolisme), Glutathione peroxidase (MeSH), Liaison aux protéines (MeSH), Prions (métabolisme), Protéines de Saccharomyces cerevisiae (analyse), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de répression (analyse), Protéines de répression (métabolisme), Saccharomyces cerevisiae (métabolisme), Sirolimus (métabolisme), Sites de fixation (MeSH), Structure tertiaire des protéines (MeSH).
MESH :
- analyse : Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Protéines de répression.
- métabolisme : Caryophérines, Facteurs de transcription, Prions, Protéines de Saccharomyces cerevisiae, Protéines de répression, Saccharomyces cerevisiae, Sirolimus.
- Glutathione peroxidase, Liaison aux protéines, Sites de fixation, Structure tertiaire des protéines.

English descriptors

KwdEn :
- Binding Sites (MeSH), Glutathione Peroxidase (MeSH), Karyopherins (metabolism), Prions (metabolism), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Repressor Proteins (analysis), Repressor Proteins (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (analysis), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (metabolism), Transcription Factors (analysis), Transcription Factors (metabolism).
MESH :
- chemical , analysis : Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : Karyopherins, Prions, Repressor Proteins, Saccharomyces cerevisiae Proteins, Sirolimus, Transcription Factors.
- chemical : Glutathione Peroxidase.
- metabolism : Saccharomyces cerevisiae.
- Binding Sites, Protein Binding, Protein Structure, Tertiary.

Abstract

Gln3p is a GATA-type transcription factor responsive to the quality of nitrogen and carbon. In preferred nitrogen such as glutamine, Gln3p is phosphorylated and sequestered in the cytoplasm in a manner that is dependent on the target of rapamycin (TOR) protein and Ure2p. In nonpreferred nitrogen or nitrogen starvation, Gln3p is dephosphorylated and imported into the nucleus via karyopherin alpha/Srp1p. Upon reintroduction of preferred nitrogen, Gln3p is exported from the nucleus by Crm1p/Xpo1p. Although recent work has provided insights into Gln3p, a more detailed understanding is needed to elucidate the mechanism of its localization and function. In this study, we show that Gln3p contains canonical nuclear localization signal and nuclear export signal sequences necessary for its localization and interaction with its relevant karyopherins. In addition, we identify an N-terminal domain of Gln3p interacting with Ure2p and a C-terminal region for binding to TOR. Finally, we find a lysine/arginine-rich domain essential for the rapamycin-sensitive function, but dispensable for its localization. Our results reveal key domains of Gln3p important for its function and regulation.

DOI: 10.1074/jbc.M300429200
PubMed: 12624103

Affiliations:

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Le document en format XML

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<wicri:regionArea>Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110</wicri:regionArea>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Glutathione Peroxidase (MeSH)</term>
<term>Karyopherins (metabolism)</term>
<term>Prions (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Repressor Proteins (analysis)</term>
<term>Repressor Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (analysis)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Sirolimus (metabolism)</term>
<term>Transcription Factors (analysis)</term>
<term>Transcription Factors (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Caryophérines (métabolisme)</term>
<term>Facteurs de transcription (analyse)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Glutathione peroxidase (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Prions (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (analyse)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de répression (analyse)</term>
<term>Protéines de répression (métabolisme)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sirolimus (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Repressor Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Karyopherins</term>
<term>Prions</term>
<term>Repressor Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Sirolimus</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutathione Peroxidase</term>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de répression</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Caryophérines</term>
<term>Facteurs de transcription</term>
<term>Prions</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de répression</term>
<term>Saccharomyces cerevisiae</term>
<term>Sirolimus</term>
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<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Glutathione peroxidase</term>
<term>Liaison aux protéines</term>
<term>Sites de fixation</term>
<term>Structure tertiaire des protéines</term>
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<front><div type="abstract" xml:lang="en">Gln3p is a GATA-type transcription factor responsive to the quality of nitrogen and carbon. In preferred nitrogen such as glutamine, Gln3p is phosphorylated and sequestered in the cytoplasm in a manner that is dependent on the target of rapamycin (TOR) protein and Ure2p. In nonpreferred nitrogen or nitrogen starvation, Gln3p is dephosphorylated and imported into the nucleus via karyopherin alpha/Srp1p. Upon reintroduction of preferred nitrogen, Gln3p is exported from the nucleus by Crm1p/Xpo1p. Although recent work has provided insights into Gln3p, a more detailed understanding is needed to elucidate the mechanism of its localization and function. In this study, we show that Gln3p contains canonical nuclear localization signal and nuclear export signal sequences necessary for its localization and interaction with its relevant karyopherins. In addition, we identify an N-terminal domain of Gln3p interacting with Ure2p and a C-terminal region for binding to TOR. Finally, we find a lysine/arginine-rich domain essential for the rapamycin-sensitive function, but dispensable for its localization. Our results reveal key domains of Gln3p important for its function and regulation.</div>
</front>
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<Abstract><AbstractText>Gln3p is a GATA-type transcription factor responsive to the quality of nitrogen and carbon. In preferred nitrogen such as glutamine, Gln3p is phosphorylated and sequestered in the cytoplasm in a manner that is dependent on the target of rapamycin (TOR) protein and Ure2p. In nonpreferred nitrogen or nitrogen starvation, Gln3p is dephosphorylated and imported into the nucleus via karyopherin alpha/Srp1p. Upon reintroduction of preferred nitrogen, Gln3p is exported from the nucleus by Crm1p/Xpo1p. Although recent work has provided insights into Gln3p, a more detailed understanding is needed to elucidate the mechanism of its localization and function. In this study, we show that Gln3p contains canonical nuclear localization signal and nuclear export signal sequences necessary for its localization and interaction with its relevant karyopherins. In addition, we identify an N-terminal domain of Gln3p interacting with Ure2p and a C-terminal region for binding to TOR. Finally, we find a lysine/arginine-rich domain essential for the rapamycin-sensitive function, but dispensable for its localization. Our results reveal key domains of Gln3p important for its function and regulation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Carvalho</LastName>
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<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.</Affiliation>
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<Author ValidYN="Y"><LastName>Zheng</LastName>
<ForeName>X F Steven</ForeName>
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<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01CA77668</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
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<Grant><GrantID>R01GM62817</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D028884">Karyopherins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber>
<NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber>
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<Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber>
<NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance>
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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

Domains of Gln3p interacting with karyopherins, Ure2p, and the target of rapamycin protein.

Domains of Gln3p interacting with karyopherins, Ure2p, and the target of rapamycin protein.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki