RapamycinFungusV1, Main, Exploration, bibRecord, 000469

Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.

Identifieur interne : 000469 ( Main/Exploration ); précédent : 000468; suivant : 000470

Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.

Auteurs : Maristella De Cicco [Allemagne] ; Lech-G Milroy [Pays-Bas] ; Sonja A. Dames [Allemagne]

Source :

Protein science : a publication of the Protein Society [ 1469-896X ] ; 2018.

RBID : pubmed:29024217

Descripteurs français

English descriptors

KwdEn :
- Cell Membrane (metabolism), Circular Dichroism (MeSH), Humans (MeSH), Liposomes (metabolism), Micelles (MeSH), Models, Molecular (MeSH), Molecular Dynamics Simulation (MeSH), Mutation (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Phosphatidylinositol 3-Kinases (chemistry), Phosphatidylinositol 3-Kinases (genetics), Phosphatidylinositol 3-Kinases (metabolism), Protein Conformation (MeSH), Protein Domains (MeSH), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Tacrolimus Binding Proteins (chemistry), Tacrolimus Binding Proteins (genetics), Tacrolimus Binding Proteins (metabolism).
MESH :
- chemical , chemistry : Phosphatidylinositol 3-Kinases, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Tacrolimus Binding Proteins.
- chemical , genetics : Phosphatidylinositol 3-Kinases, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Tacrolimus Binding Proteins.
- chemical , metabolism : Liposomes, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins, Tacrolimus Binding Proteins.
- chemistry : Saccharomyces cerevisiae.
- metabolism : Cell Membrane, Saccharomyces cerevisiae.
- Circular Dichroism, Humans, Micelles, Models, Molecular, Molecular Dynamics Simulation, Mutation, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Domains.

Abstract

Increased efforts have been undertaken to better understand the formation of signaling complexes at cellular membranes. Since the preparation of proteins containing a transmembrane domain or a prenylation motif is generally challenging an alternative membrane anchoring unit that is easy to attach, water-soluble and binds to different membrane mimetics would find broad application. The 33-residue long FATC domain of yeast TOR1 (y1fatc) fulfills these criteria and binds to neutral and negatively charged micelles, bicelles, and liposomes. As a case study, we fused it to the FKBP506-binding region of the protein FKBP38 (FKBP38-BD) and used ¹ H-¹⁵ N NMR spectroscopy to characterize localization of the chimeric protein to micelles, bicelles, and liposomes. Based on these and published data for y1fatc, its use as a C-terminally attachable membrane anchor for other proteins is compatible with a wide range of buffer conditions (pH circa 6-8.5, NaCl 0 to >150 mM, presence of reducing agents, different salts such as MgCl₂ and CaCl₂ ). The high water-solubility of y1fatc enables its use for titration experiments against a membrane-localized interaction partner of the fused target protein. Results from studies with peptides corresponding to the C-terminal 17-11 residues of the 33-residue long domain by 1D ¹ H NMR and CD spectroscopy indicate that they still can interact with membrane mimetics. Thus, they may be used as membrane anchors if the full y1fatc sequence is disturbing or if a chemically synthesized y1fatc peptide shall be attached by native chemical ligation, for example, unlabeled peptide to ¹⁵ N-labeled target protein for NMR studies.

DOI: 10.1002/pro.3321
PubMed: 29024217
PubMed Central: PMC5775168

Affiliations:

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

to stream Main, to step Corpus: 000704
to stream Main, to step Curation: 000704

Le document en format XML

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<term>Humans (MeSH)</term>
<term>Liposomes (metabolism)</term>
<term>Micelles (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Dynamics Simulation (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term>
<term>Phosphatidylinositol 3-Kinases (chemistry)</term>
<term>Phosphatidylinositol 3-Kinases (genetics)</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Protein Conformation (MeSH)</term>
<term>Protein Domains (MeSH)</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Saccharomyces cerevisiae (chemistry)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Tacrolimus Binding Proteins (chemistry)</term>
<term>Tacrolimus Binding Proteins (genetics)</term>
<term>Tacrolimus Binding Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term>
<term>Dichroïsme circulaire (MeSH)</term>
<term>Domaines protéiques (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Liposomes (métabolisme)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Micelles (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Phosphatidylinositol 3-kinases (composition chimique)</term>
<term>Phosphatidylinositol 3-kinases (génétique)</term>
<term>Phosphatidylinositol 3-kinases (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de fusion recombinantes (composition chimique)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de liaison au tacrolimus (composition chimique)</term>
<term>Protéines de liaison au tacrolimus (génétique)</term>
<term>Protéines de liaison au tacrolimus (métabolisme)</term>
<term>Résonance magnétique nucléaire biomoléculaire (MeSH)</term>
<term>Saccharomyces cerevisiae (composition chimique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Simulation de dynamique moléculaire (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Phosphatidylinositol 3-Kinases</term>
<term>Recombinant Fusion Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Tacrolimus Binding Proteins</term>
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<term>Recombinant Fusion Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Tacrolimus Binding Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Liposomes</term>
<term>Phosphatidylinositol 3-Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Tacrolimus Binding Proteins</term>
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<term>Protéines de fusion recombinantes</term>
<term>Protéines de liaison au tacrolimus</term>
<term>Saccharomyces cerevisiae</term>
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<term>Protéines de fusion recombinantes</term>
<term>Protéines de liaison au tacrolimus</term>
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<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Liposomes</term>
<term>Membrane cellulaire</term>
<term>Phosphatidylinositol 3-kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de liaison au tacrolimus</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term>
<term>Humans</term>
<term>Micelles</term>
<term>Models, Molecular</term>
<term>Molecular Dynamics Simulation</term>
<term>Mutation</term>
<term>Nuclear Magnetic Resonance, Biomolecular</term>
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<term>Humains</term>
<term>Micelles</term>
<term>Modèles moléculaires</term>
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<front><div type="abstract" xml:lang="en">Increased efforts have been undertaken to better understand the formation of signaling complexes at cellular membranes. Since the preparation of proteins containing a transmembrane domain or a prenylation motif is generally challenging an alternative membrane anchoring unit that is easy to attach, water-soluble and binds to different membrane mimetics would find broad application. The 33-residue long FATC domain of yeast TOR1 (y1fatc) fulfills these criteria and binds to neutral and negatively charged micelles, bicelles, and liposomes. As a case study, we fused it to the FKBP506-binding region of the protein FKBP38 (FKBP38-BD) and used <sup>1</sup>
 H-<sup>15</sup>
 N NMR spectroscopy to characterize localization of the chimeric protein to micelles, bicelles, and liposomes. Based on these and published data for y1fatc, its use as a C-terminally attachable membrane anchor for other proteins is compatible with a wide range of buffer conditions (pH circa 6-8.5, NaCl 0 to >150 mM, presence of reducing agents, different salts such as MgCl<sub>2</sub>
 and CaCl<sub>2</sub>
 ). The high water-solubility of y1fatc enables its use for titration experiments against a membrane-localized interaction partner of the fused target protein. Results from studies with peptides corresponding to the C-terminal 17-11 residues of the 33-residue long domain by 1D <sup>1</sup>
 H NMR and CD spectroscopy indicate that they still can interact with membrane mimetics. Thus, they may be used as membrane anchors if the full y1fatc sequence is disturbing or if a chemically synthesized y1fatc peptide shall be attached by native chemical ligation, for example, unlabeled peptide to <sup>15</sup>
 N-labeled target protein for NMR studies.</div>
</front>
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<Abstract><AbstractText>Increased efforts have been undertaken to better understand the formation of signaling complexes at cellular membranes. Since the preparation of proteins containing a transmembrane domain or a prenylation motif is generally challenging an alternative membrane anchoring unit that is easy to attach, water-soluble and binds to different membrane mimetics would find broad application. The 33-residue long FATC domain of yeast TOR1 (y1fatc) fulfills these criteria and binds to neutral and negatively charged micelles, bicelles, and liposomes. As a case study, we fused it to the FKBP506-binding region of the protein FKBP38 (FKBP38-BD) and used <sup>1</sup>
 H-<sup>15</sup>
 N NMR spectroscopy to characterize localization of the chimeric protein to micelles, bicelles, and liposomes. Based on these and published data for y1fatc, its use as a C-terminally attachable membrane anchor for other proteins is compatible with a wide range of buffer conditions (pH circa 6-8.5, NaCl 0 to >150 mM, presence of reducing agents, different salts such as MgCl<sub>2</sub>
 and CaCl<sub>2</sub>
 ). The high water-solubility of y1fatc enables its use for titration experiments against a membrane-localized interaction partner of the fused target protein. Results from studies with peptides corresponding to the C-terminal 17-11 residues of the 33-residue long domain by 1D <sup>1</sup>
 H NMR and CD spectroscopy indicate that they still can interact with membrane mimetics. Thus, they may be used as membrane anchors if the full y1fatc sequence is disturbing or if a chemically synthesized y1fatc peptide shall be attached by native chemical ligation, for example, unlabeled peptide to <sup>15</sup>
 N-labeled target protein for NMR studies.</AbstractText>
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<ForeName>Maristella</ForeName>
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<ForeName>Sonja A</ForeName>
<Initials>SA</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, Technische Universität München, Biomolecular NMR Spectroscopy, Garching, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany.</Affiliation>
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<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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	Serveur d'exploration sur la rapamycine et les champignons
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Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.

Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.

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