Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
Identifieur interne : 002451 ( Main/Exploration ); précédent : 002450; suivant : 002452Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
Auteurs : Justyna Sawa [Autriche] ; Hélène Malet ; Tobias Krojer ; Flavia Canellas ; Michael Ehrmann ; Tim ClausenSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2011.
Descripteurs français
- KwdFr :
- Calorimétrie (), Chromatographie sur gel, Concentration en ions d'hydrogène, Conformation moléculaire, Cristallisation, Cristallographie aux rayons X (), Liaison aux protéines, Membrane cellulaire (métabolisme), Protéases à sérine (), Protéines Escherichia coli (), Protéines Escherichia coli (physiologie), Protéines bactériennes (métabolisme), Protéines du choc thermique (métabolisme), Protéines périplasmiques (métabolisme), Serine endopeptidases (), Serine endopeptidases (métabolisme), Serine endopeptidases (physiologie), Site allostérique, Structure tertiaire des protéines, Thermodynamique.
- MESH :
- métabolisme : Membrane cellulaire, Protéines bactériennes, Protéines du choc thermique, Protéines périplasmiques, Serine endopeptidases.
- physiologie : Protéines Escherichia coli, Serine endopeptidases.
- Calorimétrie, Chromatographie sur gel, Concentration en ions d'hydrogène, Conformation moléculaire, Cristallisation, Cristallographie aux rayons X, Liaison aux protéines, Protéases à sérine, Protéines Escherichia coli, Serine endopeptidases, Site allostérique, Structure tertiaire des protéines, Thermodynamique.
English descriptors
- KwdEn :
- Allosteric Site, Bacterial Proteins (metabolism), Calorimetry (methods), Cell Membrane (metabolism), Chromatography, Gel, Crystallization, Crystallography, X-Ray (methods), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (physiology), Heat-Shock Proteins (metabolism), Hydrogen-Ion Concentration, Molecular Conformation, Periplasmic Proteins (metabolism), Protein Binding, Protein Structure, Tertiary, Serine Endopeptidases (chemistry), Serine Endopeptidases (metabolism), Serine Endopeptidases (physiology), Serine Proteases (chemistry), Thermodynamics.
- MESH :
- chemical , chemistry : Escherichia coli Proteins, Serine Endopeptidases, Serine Proteases.
- chemical , metabolism : Bacterial Proteins, Heat-Shock Proteins, Periplasmic Proteins, Serine Endopeptidases.
- metabolism : Cell Membrane.
- methods : Calorimetry, Crystallography, X-Ray.
- chemical , physiology : Escherichia coli Proteins, Serine Endopeptidases.
- Allosteric Site, Chromatography, Gel, Crystallization, Hydrogen-Ion Concentration, Molecular Conformation, Protein Binding, Protein Structure, Tertiary, Thermodynamics.
Abstract
To react to distinct stress situations and to prevent the accumulation of misfolded proteins, all cells employ a number of proteases and chaperones, which together set up an efficient protein quality control system. The functionality of proteins in the cell envelope of Escherichia coli is monitored by the HtrA proteases DegS, DegP, and DegQ. In contrast with DegP and DegS, the structure and function of DegQ has not been addressed in detail. Here, we show that substrate binding triggers the conversion of the resting DegQ hexamer into catalytically active 12- and 24-mers. Interestingly, substrate-induced oligomer reassembly and protease activation depends on the first PDZ domain but not on the second. Therefore, the regulatory mechanism originally identified in DegP should be a common feature of HtrA proteases, most of which encompass only a single PDZ domain. Using a DegQ mutant lacking the second PDZ domain, we determined the high resolution crystal structure of a dodecameric HtrA complex. The nearly identical domain orientation of protease and PDZ domains within 12- and 24-meric HtrA complexes reveals a conserved PDZ1 → L3 → LD/L1/L2 signaling cascade, in which loop L3 senses the repositioned PDZ1 domain of higher order, substrate-engaged particles and activates protease function. Furthermore, our in vitro and in vivo data imply a pH-related function of DegQ in the bacterial cell envelope.
DOI: 10.1074/jbc.M111.243832
PubMed: 21685389
Affiliations:
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Le document en format XML
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The functionality of proteins in the cell envelope of Escherichia coli is monitored by the HtrA proteases DegS, DegP, and DegQ. In contrast with DegP and DegS, the structure and function of DegQ has not been addressed in detail. Here, we show that substrate binding triggers the conversion of the resting DegQ hexamer into catalytically active 12- and 24-mers. Interestingly, substrate-induced oligomer reassembly and protease activation depends on the first PDZ domain but not on the second. Therefore, the regulatory mechanism originally identified in DegP should be a common feature of HtrA proteases, most of which encompass only a single PDZ domain. Using a DegQ mutant lacking the second PDZ domain, we determined the high resolution crystal structure of a dodecameric HtrA complex. The nearly identical domain orientation of protease and PDZ domains within 12- and 24-meric HtrA complexes reveals a conserved PDZ1 → L3 → LD/L1/L2 signaling cascade, in which loop L3 senses the repositioned PDZ1 domain of higher order, substrate-engaged particles and activates protease function. Furthermore, our in vitro and in vivo data imply a pH-related function of DegQ in the bacterial cell envelope.</div></front></TEI><affiliations><list><country><li>Autriche</li></country></list><tree><noCountry><name sortKey="Canellas, Flavia" sort="Canellas, Flavia" uniqKey="Canellas F" first="Flavia" last="Canellas">Flavia Canellas</name><name sortKey="Clausen, Tim" sort="Clausen, Tim" uniqKey="Clausen T" first="Tim" last="Clausen">Tim Clausen</name><name sortKey="Ehrmann, Michael" sort="Ehrmann, Michael" uniqKey="Ehrmann M" first="Michael" last="Ehrmann">Michael Ehrmann</name><name sortKey="Krojer, Tobias" sort="Krojer, Tobias" uniqKey="Krojer T" first="Tobias" last="Krojer">Tobias Krojer</name><name sortKey="Malet, Helene" sort="Malet, Helene" uniqKey="Malet H" first="Hélène" last="Malet">Hélène Malet</name></noCountry><country name="Autriche"><noRegion><name sortKey="Sawa, Justyna" sort="Sawa, Justyna" uniqKey="Sawa J" first="Justyna" last="Sawa">Justyna Sawa</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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