RapamycinFungusV1, Main, Exploration, bibRecord, 000F35

A domain in the transcription activator Gln3 specifically required for rapamycin responsiveness.

Identifieur interne : 000F35 ( Main/Exploration ); précédent : 000F34; suivant : 000F36

A domain in the transcription activator Gln3 specifically required for rapamycin responsiveness.

Auteurs : Rajendra Rai [États-Unis] ; Jennifer J. Tate [États-Unis] ; Karthik Shanmuganatham [États-Unis] ; Martha M. Howe [États-Unis] ; Terrance G. Cooper [États-Unis]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2014.

RBID : pubmed:24847055

Descripteurs français

KwdFr :
- Données de séquences moléculaires (MeSH), Facteurs de transcription (composition chimique), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Modèles moléculaires (MeSH), Mutation (MeSH), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Résistance des champignons aux médicaments (génétique), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Structure tertiaire des protéines (MeSH), Substitution d'acide aminé (MeSH), Séquence d'acides aminés (MeSH), Transport des protéines (effets des médicaments et des substances chimiques).
MESH :
- composition chimique : Facteurs de transcription, Protéines de Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae, Transport des protéines.
- génétique : Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Résistance des champignons aux médicaments, Saccharomyces cerevisiae.
- métabolisme : Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- Données de séquences moléculaires, Modèles moléculaires, Mutation, Structure tertiaire des protéines, Substitution d'acide aminé, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Amino Acid Substitution (MeSH), Drug Resistance, Fungal (genetics), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Protein Structure, Tertiary (MeSH), Protein Transport (drug effects), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Transcription Factors (chemistry), Transcription Factors (genetics), Transcription Factors (metabolism).
MESH :
- chemical , chemistry : Saccharomyces cerevisiae Proteins, Transcription Factors.
- drug effects : Protein Transport, Saccharomyces cerevisiae.
- genetics : Drug Resistance, Fungal, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors.
- metabolism : Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Sirolimus.
- Amino Acid Sequence, Amino Acid Substitution, Models, Molecular, Molecular Sequence Data, Mutation, Protein Structure, Tertiary.

Abstract

Nitrogen-responsive control of Gln3 localization is implemented through TorC1-dependent (rapamycin-responsive) and TorC1-independent (nitrogen catabolite repression-sensitive and methionine sulfoximine (Msx)-responsive) regulatory pathways. We previously demonstrated amino acid substitutions in a putative Gln3 α-helix(656-666), which are required for a two-hybrid Gln3-Tor1 interaction, also abolished rapamycin responsiveness of Gln3 localization and partially abrogated cytoplasmic Gln3 sequestration in cells cultured under nitrogen-repressive conditions. Here, we demonstrate these three characteristics are not inextricably linked together. A second distinct Gln3 region (Gln3(510-589)) is specifically required for rapamycin responsiveness of Gln3 localization, but not for cytoplasmic Gln3 sequestration under repressive growth conditions or relocation to the nucleus following Msx addition. Aspartate or alanine substitution mutations throughout this region uniformly abolish rapamycin responsiveness. Contained within this region is a sequence with a predicted propensity to form an α-helix(583-591), one side of which consists of three hydrophobic amino acids flanked by serine residues. Substitution of aspartate for even one of these serines abolishes rapamycin responsiveness and increases rapamycin resistance without affecting either of the other two Gln3 localization responses. In contrast, alanine substitutions decrease rapamycin resistance. Together, these data suggest that targets in the C-terminal portion of Gln3 required for the Gln3-Tor1 interaction, cytoplasmic Gln3 sequestration, and Gln3 responsiveness to Msx addition and growth in poor nitrogen sources are distinct from those needed for rapamycin responsiveness.

DOI: 10.1074/jbc.M114.563668
PubMed: 24847055
PubMed Central: PMC4081939

Affiliations:

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

to stream Main, to step Corpus: 000E45
to stream Main, to step Curation: 000E45

Le document en format XML

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<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Mutation (MeSH)</term>
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<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Nitrogen-responsive control of Gln3 localization is implemented through TorC1-dependent (rapamycin-responsive) and TorC1-independent (nitrogen catabolite repression-sensitive and methionine sulfoximine (Msx)-responsive) regulatory pathways. We previously demonstrated amino acid substitutions in a putative Gln3 α-helix(656-666), which are required for a two-hybrid Gln3-Tor1 interaction, also abolished rapamycin responsiveness of Gln3 localization and partially abrogated cytoplasmic Gln3 sequestration in cells cultured under nitrogen-repressive conditions. Here, we demonstrate these three characteristics are not inextricably linked together. A second distinct Gln3 region (Gln3(510-589)) is specifically required for rapamycin responsiveness of Gln3 localization, but not for cytoplasmic Gln3 sequestration under repressive growth conditions or relocation to the nucleus following Msx addition. Aspartate or alanine substitution mutations throughout this region uniformly abolish rapamycin responsiveness. Contained within this region is a sequence with a predicted propensity to form an α-helix(583-591), one side of which consists of three hydrophobic amino acids flanked by serine residues. Substitution of aspartate for even one of these serines abolishes rapamycin responsiveness and increases rapamycin resistance without affecting either of the other two Gln3 localization responses. In contrast, alanine substitutions decrease rapamycin resistance. Together, these data suggest that targets in the C-terminal portion of Gln3 required for the Gln3-Tor1 interaction, cytoplasmic Gln3 sequestration, and Gln3 responsiveness to Msx addition and growth in poor nitrogen sources are distinct from those needed for rapamycin responsiveness. </div>
</front>
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<DateCompleted><Year>2014</Year>
<Month>10</Month>
<Day>14</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
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<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
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<ArticleTitle>A domain in the transcription activator Gln3 specifically required for rapamycin responsiveness.</ArticleTitle>
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<Abstract><AbstractText>Nitrogen-responsive control of Gln3 localization is implemented through TorC1-dependent (rapamycin-responsive) and TorC1-independent (nitrogen catabolite repression-sensitive and methionine sulfoximine (Msx)-responsive) regulatory pathways. We previously demonstrated amino acid substitutions in a putative Gln3 α-helix(656-666), which are required for a two-hybrid Gln3-Tor1 interaction, also abolished rapamycin responsiveness of Gln3 localization and partially abrogated cytoplasmic Gln3 sequestration in cells cultured under nitrogen-repressive conditions. Here, we demonstrate these three characteristics are not inextricably linked together. A second distinct Gln3 region (Gln3(510-589)) is specifically required for rapamycin responsiveness of Gln3 localization, but not for cytoplasmic Gln3 sequestration under repressive growth conditions or relocation to the nucleus following Msx addition. Aspartate or alanine substitution mutations throughout this region uniformly abolish rapamycin responsiveness. Contained within this region is a sequence with a predicted propensity to form an α-helix(583-591), one side of which consists of three hydrophobic amino acids flanked by serine residues. Substitution of aspartate for even one of these serines abolishes rapamycin responsiveness and increases rapamycin resistance without affecting either of the other two Gln3 localization responses. In contrast, alanine substitutions decrease rapamycin resistance. Together, these data suggest that targets in the C-terminal portion of Gln3 required for the Gln3-Tor1 interaction, cytoplasmic Gln3 sequestration, and Gln3 responsiveness to Msx addition and growth in poor nitrogen sources are distinct from those needed for rapamycin responsiveness. </AbstractText>
<CopyrightInformation>© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation>
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<ForeName>Rajendra</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>From the Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163 and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tate</LastName>
<ForeName>Jennifer J</ForeName>
<Initials>JJ</Initials>
<AffiliationInfo><Affiliation>From the Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163 and.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Shanmuganatham</LastName>
<ForeName>Karthik</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>the Division of Virology, Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.</Affiliation>
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<AffiliationInfo><Affiliation>From the Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163 and.</Affiliation>
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<ForeName>Terrance G</ForeName>
<Initials>TG</Initials>
<AffiliationInfo><Affiliation>From the Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163 and tcooper@uthsc.edu.</Affiliation>
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<NameOfSubstance UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance>
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<MeshHeading><DescriptorName UI="D025141" MajorTopicYN="N">Drug Resistance, Fungal</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
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<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
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<MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName>
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<MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName>
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<MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Nitrogen Metabolism</Keyword>
<Keyword MajorTopicYN="N">Nuclear Translocation</Keyword>
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	Serveur d'exploration sur la rapamycine et les champignons
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A domain in the transcription activator Gln3 specifically required for rapamycin responsiveness.

A domain in the transcription activator Gln3 specifically required for rapamycin responsiveness.

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