Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
Identifieur interne : 001E66 ( PubMed/Corpus ); précédent : 001E65; suivant : 001E67Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
Auteurs : Justyna Sawa ; Hélène Malet ; Tobias Krojer ; Flavia Canellas ; Michael Ehrmann ; Tim ClausenSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2011.
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
Links to Exploration step
pubmed:21685389Le document en format XML
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Helene" sort="Malet, Helene" uniqKey="Malet H" first="Hélène" last="Malet">Hélène Malet</name></author><author><name sortKey="Krojer, Tobias" sort="Krojer, Tobias" uniqKey="Krojer T" first="Tobias" last="Krojer">Tobias Krojer</name></author><author><name sortKey="Canellas, Flavia" sort="Canellas, Flavia" uniqKey="Canellas F" first="Flavia" last="Canellas">Flavia Canellas</name></author><author><name sortKey="Ehrmann, Michael" sort="Ehrmann, Michael" uniqKey="Ehrmann M" first="Michael" last="Ehrmann">Michael Ehrmann</name></author><author><name sortKey="Clausen, Tim" sort="Clausen, Tim" uniqKey="Clausen T" first="Tim" last="Clausen">Tim Clausen</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Site</term><term>Bacterial 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qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Heat-Shock Proteins</term><term>Periplasmic Proteins</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Calorimetry</term><term>Crystallography, X-Ray</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Escherichia coli Proteins</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Allosteric Site</term><term>Chromatography, Gel</term><term>Crystallization</term><term>Hydrogen-Ion Concentration</term><term>Molecular Conformation</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Thermodynamics</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21685389</PMID><DateCompleted><Year>2011</Year><Month>10</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>286</Volume><Issue>35</Issue><PubDate><Year>2011</Year><Month>Sep</Month><Day>02</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.</ArticleTitle><Pagination><MedlinePgn>30680-90</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M111.243832</ELocationID><Abstract><AbstractText>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. 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|texte= Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
}}
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| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
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