Substrate occupancy at the onset of oligomeric transitions of DegP.
Identifieur interne : 001A72 ( Main/Exploration ); précédent : 001A71; suivant : 001A73Substrate occupancy at the onset of oligomeric transitions of DegP.
Auteurs : Natalie J. Thompson [Pays-Bas] ; Melisa Merdanovic [Allemagne] ; Michael Ehrmann [Royaume-Uni] ; Esther Van Duijn [Pays-Bas] ; Albert J R. Heck [Pays-Bas]Source :
- Structure (London, England : 1993) [ 1878-4186 ] ; 2014.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires, Escherichia coli (enzymologie), Liaison aux protéines, Ligands, Peptides (), Pliage des protéines, Protéines du choc thermique (), Protéines périplasmiques (), Serine endopeptidases (), Spectrométrie de masse, Spécificité du substrat, Structure quaternaire des protéines, Séquence d'acides aminés.
- MESH :
- enzymologie : Escherichia coli.
- Données de séquences moléculaires, Liaison aux protéines, Ligands, Peptides, Pliage des protéines, Protéines du choc thermique, Protéines périplasmiques, Serine endopeptidases, Spectrométrie de masse, Spécificité du substrat, Structure quaternaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Escherichia coli (enzymology), Heat-Shock Proteins (chemistry), Ligands, Mass Spectrometry, Molecular Sequence Data, Peptides (chemistry), Periplasmic Proteins (chemistry), Protein Binding, Protein Folding, Protein Structure, Quaternary, Serine Endopeptidases (chemistry), Substrate Specificity.
- MESH :
- chemical , chemistry : Heat-Shock Proteins, Peptides, Periplasmic Proteins, Serine Endopeptidases.
- enzymology : Escherichia coli.
- Amino Acid Sequence, Ligands, Mass Spectrometry, Molecular Sequence Data, Protein Binding, Protein Folding, Protein Structure, Quaternary, Substrate Specificity.
Abstract
The protease-chaperone DegP undergoes secondary through quaternary structural changes, regulating function and preventing indiscriminate proteolysis. Several structures of DegP oligomers have been observed, including the resting state 6-mer and the 12-mer and 24-mer active states. However, the precise events of the transition between the resting and active states still need to be elucidated. We used native mass spectrometry to demonstrate that binding of multiple substrate-mimicking peptide ligands to the DegP resting state occurs prior to the transition to an active conformation. This transition occurred at a 6-mer occupancy of 40% for each peptide ligand. We observed ligand-specific 9-mer formation with a maximum load of 9 peptides, whereas other substrates led to 12-mers accommodating 24 peptides. Based on these data, we present a model for the initial steps of substrate-induced transitions from the resting to active states of DegP.
DOI: 10.1016/j.str.2013.11.010
PubMed: 24373769
Affiliations:
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Thompson</name><affiliation wicri:level="4"><nlm:affiliation>Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, the Netherlands.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Pays-Bas</country><wicri:regionArea>Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht</wicri:regionArea><orgName type="university">Université d'Utrecht</orgName><placeName><settlement type="city">Utrecht</settlement><region nuts="2">Utrecht (province)</region></placeName></affiliation></author><author><name sortKey="Merdanovic, Melisa" sort="Merdanovic, Melisa" uniqKey="Merdanovic M" first="Melisa" last="Merdanovic">Melisa Merdanovic</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Biology, Center for Medical Biotechnology, University Duisburg-Essen, 45117 Essen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Faculty of Biology, Center for Medical Biotechnology, University Duisburg-Essen, 45117 Essen</wicri:regionArea><wicri:noRegion>45117 Essen</wicri:noRegion><wicri:noRegion>45117 Essen</wicri:noRegion><wicri:noRegion>45117 Essen</wicri:noRegion></affiliation></author><author><name sortKey="Ehrmann, Michael" sort="Ehrmann, Michael" uniqKey="Ehrmann M" first="Michael" last="Ehrmann">Michael Ehrmann</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Biology, Center for Medical Biotechnology, University Duisburg-Essen, 45117 Essen, Germany; School of Biosciences, Cardiff University, Cardiff CF10 3US, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Faculty of Biology, Center for Medical Biotechnology, University Duisburg-Essen, 45117 Essen, Germany; School of Biosciences, Cardiff University, Cardiff CF10 3US</wicri:regionArea><wicri:noRegion>Cardiff CF10 3US</wicri:noRegion></affiliation></author><author><name sortKey="Van Duijn, Esther" sort="Van Duijn, Esther" uniqKey="Van Duijn E" first="Esther" last="Van Duijn">Esther Van Duijn</name><affiliation wicri:level="4"><nlm:affiliation>Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, the Netherlands.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Pays-Bas</country><wicri:regionArea>Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht</wicri:regionArea><orgName type="university">Université d'Utrecht</orgName><placeName><settlement type="city">Utrecht</settlement><region nuts="2">Utrecht (province)</region></placeName></affiliation></author><author><name sortKey="Heck, Albert J R" sort="Heck, Albert J R" uniqKey="Heck A" first="Albert J R" last="Heck">Albert J R. Heck</name><affiliation wicri:level="4"><nlm:affiliation>Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, the Netherlands. Electronic address: a.j.r.heck@uu.nl.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Pays-Bas</country><wicri:regionArea>Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands; Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht</wicri:regionArea><orgName type="university">Université d'Utrecht</orgName><placeName><settlement type="city">Utrecht</settlement><region nuts="2">Utrecht (province)</region></placeName></affiliation></author></analytic><series><title level="j">Structure (London, England : 1993)</title><idno type="eISSN">1878-4186</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Escherichia coli (enzymology)</term><term>Heat-Shock Proteins (chemistry)</term><term>Ligands</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Peptides (chemistry)</term><term>Periplasmic Proteins (chemistry)</term><term>Protein Binding</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Serine Endopeptidases (chemistry)</term><term>Substrate Specificity</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Escherichia coli (enzymologie)</term><term>Liaison aux protéines</term><term>Ligands</term><term>Peptides ()</term><term>Pliage des protéines</term><term>Protéines du choc thermique ()</term><term>Protéines périplasmiques ()</term><term>Serine endopeptidases ()</term><term>Spectrométrie de masse</term><term>Spécificité du substrat</term><term>Structure quaternaire des protéines</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Heat-Shock Proteins</term><term>Peptides</term><term>Periplasmic Proteins</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Ligands</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Ligands</term><term>Peptides</term><term>Pliage des protéines</term><term>Protéines du choc thermique</term><term>Protéines périplasmiques</term><term>Serine endopeptidases</term><term>Spectrométrie de masse</term><term>Spécificité du substrat</term><term>Structure quaternaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The protease-chaperone DegP undergoes secondary through quaternary structural changes, regulating function and preventing indiscriminate proteolysis. Several structures of DegP oligomers have been observed, including the resting state 6-mer and the 12-mer and 24-mer active states. However, the precise events of the transition between the resting and active states still need to be elucidated. We used native mass spectrometry to demonstrate that binding of multiple substrate-mimicking peptide ligands to the DegP resting state occurs prior to the transition to an active conformation. This transition occurred at a 6-mer occupancy of 40% for each peptide ligand. We observed ligand-specific 9-mer formation with a maximum load of 9 peptides, whereas other substrates led to 12-mers accommodating 24 peptides. Based on these data, we present a model for the initial steps of substrate-induced transitions from the resting to active states of DegP. </div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Pays-Bas</li><li>Royaume-Uni</li></country><region><li>Utrecht (province)</li></region><settlement><li>Utrecht</li></settlement><orgName><li>Université d'Utrecht</li></orgName></list><tree><country name="Pays-Bas"><region name="Utrecht (province)"><name sortKey="Thompson, Natalie J" sort="Thompson, Natalie J" uniqKey="Thompson N" first="Natalie J" last="Thompson">Natalie J. Thompson</name></region><name sortKey="Heck, Albert J R" sort="Heck, Albert J R" uniqKey="Heck A" first="Albert J R" last="Heck">Albert J R. Heck</name><name sortKey="Van Duijn, Esther" sort="Van Duijn, Esther" uniqKey="Van Duijn E" first="Esther" last="Van Duijn">Esther Van Duijn</name></country><country name="Allemagne"><noRegion><name sortKey="Merdanovic, Melisa" sort="Merdanovic, Melisa" uniqKey="Merdanovic M" first="Melisa" last="Merdanovic">Melisa Merdanovic</name></noRegion></country><country name="Royaume-Uni"><noRegion><name sortKey="Ehrmann, Michael" sort="Ehrmann, Michael" uniqKey="Ehrmann M" first="Michael" last="Ehrmann">Michael Ehrmann</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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