Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.
Identifieur interne : 001D66 ( PubMed/Corpus ); précédent : 001D65; suivant : 001D67Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.
Auteurs : Guido Hansen ; Rolf HilgenfeldSource :
- Cellular and molecular life sciences : CMLS [ 1420-9071 ] ; 2013.
English descriptors
- KwdEn :
- Animals, Arabidopsis Proteins (chemistry), Arabidopsis Proteins (metabolism), Bacteria (chemistry), Bacteria (metabolism), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (metabolism), Heat-Shock Proteins (chemistry), Heat-Shock Proteins (metabolism), High-Temperature Requirement A Serine Peptidase 1, High-Temperature Requirement A Serine Peptidase 2, Humans, Mitochondrial Proteins (chemistry), Mitochondrial Proteins (metabolism), Models, Molecular, PDZ Domains, Peptide Hydrolases (chemistry), Peptide Hydrolases (metabolism), Periplasmic Proteins (chemistry), Periplasmic Proteins (metabolism), Plant Proteins (chemistry), Plant Proteins (metabolism), Plants (chemistry), Plants (metabolism), Protein Folding, Serine Endopeptidases (chemistry), Serine Endopeptidases (metabolism), Stress, Physiological.
- MESH :
- chemical , chemistry : Arabidopsis Proteins, Escherichia coli Proteins, Heat-Shock Proteins, Mitochondrial Proteins, Peptide Hydrolases, Periplasmic Proteins, Plant Proteins, Serine Endopeptidases.
- chemical , metabolism : Arabidopsis Proteins, Escherichia coli Proteins, Heat-Shock Proteins, Mitochondrial Proteins, Peptide Hydrolases, Periplasmic Proteins, Plant Proteins, Serine Endopeptidases.
- chemistry : Bacteria, Plants.
- metabolism : Bacteria, Plants.
- Animals, High-Temperature Requirement A Serine Peptidase 1, High-Temperature Requirement A Serine Peptidase 2, Humans, Models, Molecular, PDZ Domains, Protein Folding, Stress, Physiological.
Abstract
Protein quality control is vital for all living cells and sophisticated molecular mechanisms have evolved to prevent the excessive accumulation of unfolded proteins. High-temperature requirement A (HtrA) proteases have been identified as important ATP-independent quality-control factors in most species. HtrA proteins harbor a serine-protease domain and at least one peptide-binding PDZ domain to ensure efficient removal of misfolded or damaged proteins. One distinctive property of HtrAs is their ability to assemble into complex oligomers. Whereas all examined HtrAs are capable of forming pyramidal 3-mers, higher-order complexes consisting of up to 24 molecules have been reported. Tight control of chaperone and protease function is of pivotal importance in preventing deleterious HtrA-protease activity. In recent years, structural biology provided detailed insights into the molecular basis of the regulatory mechanisms, which include unique intramolecular allosteric signaling cascades and the dynamic switching of oligomeric states of HtrA proteins. Based on these results, functional models for many family members have been developed. The HtrA protein family represents a remarkable example of how structural and functional diversity is attained from the assembly of simple molecular building blocks.
DOI: 10.1007/s00018-012-1076-4
PubMed: 22806565
Links to Exploration step
pubmed:22806565Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.</title><author><name sortKey="Hansen, Guido" sort="Hansen, Guido" uniqKey="Hansen G" first="Guido" last="Hansen">Guido Hansen</name><affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23538, Lübeck, Germany. hansen@biochem.uni-luebeck.de</nlm:affiliation></affiliation></author><author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:22806565</idno><idno type="pmid">22806565</idno><idno type="doi">10.1007/s00018-012-1076-4</idno><idno type="wicri:Area/PubMed/Corpus">001D66</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001D66</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.</title><author><name sortKey="Hansen, Guido" sort="Hansen, Guido" uniqKey="Hansen G" first="Guido" last="Hansen">Guido Hansen</name><affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23538, Lübeck, Germany. hansen@biochem.uni-luebeck.de</nlm:affiliation></affiliation></author><author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name></author></analytic><series><title level="j">Cellular and molecular life sciences : CMLS</title><idno type="eISSN">1420-9071</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Arabidopsis Proteins (chemistry)</term><term>Arabidopsis Proteins (metabolism)</term><term>Bacteria (chemistry)</term><term>Bacteria (metabolism)</term><term>Escherichia coli Proteins (chemistry)</term><term>Escherichia coli Proteins (metabolism)</term><term>Heat-Shock Proteins (chemistry)</term><term>Heat-Shock Proteins (metabolism)</term><term>High-Temperature Requirement A Serine Peptidase 1</term><term>High-Temperature Requirement A Serine Peptidase 2</term><term>Humans</term><term>Mitochondrial Proteins (chemistry)</term><term>Mitochondrial Proteins (metabolism)</term><term>Models, Molecular</term><term>PDZ Domains</term><term>Peptide Hydrolases (chemistry)</term><term>Peptide Hydrolases (metabolism)</term><term>Periplasmic Proteins (chemistry)</term><term>Periplasmic Proteins (metabolism)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Plants (chemistry)</term><term>Plants (metabolism)</term><term>Protein Folding</term><term>Serine Endopeptidases (chemistry)</term><term>Serine Endopeptidases (metabolism)</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term><term>Escherichia coli Proteins</term><term>Heat-Shock Proteins</term><term>Mitochondrial Proteins</term><term>Peptide Hydrolases</term><term>Periplasmic Proteins</term><term>Plant Proteins</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>Escherichia coli Proteins</term><term>Heat-Shock Proteins</term><term>Mitochondrial Proteins</term><term>Peptide Hydrolases</term><term>Periplasmic Proteins</term><term>Plant Proteins</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bacteria</term><term>Plants</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacteria</term><term>Plants</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>High-Temperature Requirement A Serine Peptidase 1</term><term>High-Temperature Requirement A Serine Peptidase 2</term><term>Humans</term><term>Models, Molecular</term><term>PDZ Domains</term><term>Protein Folding</term><term>Stress, Physiological</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein quality control is vital for all living cells and sophisticated molecular mechanisms have evolved to prevent the excessive accumulation of unfolded proteins. High-temperature requirement A (HtrA) proteases have been identified as important ATP-independent quality-control factors in most species. HtrA proteins harbor a serine-protease domain and at least one peptide-binding PDZ domain to ensure efficient removal of misfolded or damaged proteins. One distinctive property of HtrAs is their ability to assemble into complex oligomers. Whereas all examined HtrAs are capable of forming pyramidal 3-mers, higher-order complexes consisting of up to 24 molecules have been reported. Tight control of chaperone and protease function is of pivotal importance in preventing deleterious HtrA-protease activity. In recent years, structural biology provided detailed insights into the molecular basis of the regulatory mechanisms, which include unique intramolecular allosteric signaling cascades and the dynamic switching of oligomeric states of HtrA proteins. Based on these results, functional models for many family members have been developed. The HtrA protein family represents a remarkable example of how structural and functional diversity is attained from the assembly of simple molecular building blocks.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22806565</PMID><DateCompleted><Year>2013</Year><Month>04</Month><Day>04</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1420-9071</ISSN><JournalIssue CitedMedium="Internet"><Volume>70</Volume><Issue>5</Issue><PubDate><Year>2013</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Cellular and molecular life sciences : CMLS</Title><ISOAbbreviation>Cell. Mol. Life Sci.</ISOAbbreviation></Journal><ArticleTitle>Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.</ArticleTitle><Pagination><MedlinePgn>761-75</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00018-012-1076-4</ELocationID><Abstract><AbstractText>Protein quality control is vital for all living cells and sophisticated molecular mechanisms have evolved to prevent the excessive accumulation of unfolded proteins. High-temperature requirement A (HtrA) proteases have been identified as important ATP-independent quality-control factors in most species. HtrA proteins harbor a serine-protease domain and at least one peptide-binding PDZ domain to ensure efficient removal of misfolded or damaged proteins. One distinctive property of HtrAs is their ability to assemble into complex oligomers. Whereas all examined HtrAs are capable of forming pyramidal 3-mers, higher-order complexes consisting of up to 24 molecules have been reported. Tight control of chaperone and protease function is of pivotal importance in preventing deleterious HtrA-protease activity. In recent years, structural biology provided detailed insights into the molecular basis of the regulatory mechanisms, which include unique intramolecular allosteric signaling cascades and the dynamic switching of oligomeric states of HtrA proteins. Based on these results, functional models for many family members have been developed. The HtrA protein family represents a remarkable example of how structural and functional diversity is attained from the assembly of simple molecular building blocks.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hansen</LastName><ForeName>Guido</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23538, Lübeck, Germany. hansen@biochem.uni-luebeck.de</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hilgenfeld</LastName><ForeName>Rolf</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate 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