Dis-assembly lines: the proteasome and related ATPase-assisted proteases
Identifieur interne : 002601 ( Istex/Corpus ); précédent : 002600; suivant : 002602Dis-assembly lines: the proteasome and related ATPase-assisted proteases
Auteurs : Peter Zwickl ; Wolfgang Baumeister ; Alasdair StevenSource :
- Current Opinion in Structural Biology [ 0959-440X ] ; 2000.
English descriptors
- Teeft :
- Acad, Acidophilum, Active sites, Atpase, Atpase domains, Atpases, Bacteriophage, Baumeister, Biol, Biol chem, Cell biol, Chaperone, Chem, Clpa, Clpap, Clpap protease, Clpp, Coli, Core particle, Crystal structure, Crystallographic study, Degradation, Electron microscopy, Escherichia, Escherichia coli, Eukaryotic, Febs lett, Huber, Image analysis, Lupas, Maurizi, Mismatch, Module, Mutational, Natl, Ornithine decarboxylase, Other hand, Other proteases, Peptide, Precursor, Proc, Proc natl acad, Processive, Processive degradation, Propeptides, Protease, Proteases zwickl, Proteasomal, Proteasomal atpases, Proteasome, Proteasomes, Protein breakdown, Protein degradation, Protein substrates, Proteolysis, Proteolytic, Regulator, Relative rotation, Sensitive factor, Steven, Struct biol, Structural organization, Subcomplex, Subcomplexes, Substrate binding, Substrate proteins, Subunit, Subunit composition, Symmetry mismatch, Thermoplasma, Thermoplasma acidophilum, Translocation, Type subunits, Yeast, Yeast proteasomes, Zwickl.
Abstract
Abstract: Self-compartmentalizing proteases, such as the proteasome and several prokaryotic energy-dependent proteases, are designed to act in the crowded environment of the cell. Proteins destined for degradation are recognized and unfolded by regulatory subcomplexes that invariably contain ATPase modules, before being translocated into another subcomplex, the proteolytic core, for degradation. The sequential actions effected on substrates are reflected in the linear arrangement of these subcomplexes; thus, the holocomplexes are organized as molecular disassembly and degradation lines.
Url:
DOI: 10.1016/S0959-440X(00)00075-0
Links to Exploration step
ISTEX:6B1F6DADCCD3763AC2C268DDAC9BE90AE1349E67Le document en format XML
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article</json:string></originalGenre><abstract>Abstract: Self-compartmentalizing proteases, such as the proteasome and several prokaryotic energy-dependent proteases, are designed to act in the crowded environment of the cell. Proteins destined for degradation are recognized and unfolded by regulatory subcomplexes that invariably contain ATPase modules, before being translocated into another subcomplex, the proteolytic core, for degradation. The sequential actions effected on substrates are reflected in the linear arrangement of these subcomplexes; thus, the holocomplexes are organized as molecular disassembly and degradation lines.</abstract><qualityIndicators><score>7.912</score><pdfWordCount>7187</pdfWordCount><pdfCharCount>46268</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>9</pdfPageCount><pdfPageSize>612 x 794 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>76</abstractWordCount><abstractCharCount>593</abstractCharCount><keywordCount>12</keywordCount></qualityIndicators><title>Dis-assembly lines: the proteasome and related ATPase-assisted proteases</title><pmid><json:string>10753810</json:string></pmid><pii><json:string>S0959-440X(00)00075-0</json:string></pii><genre><json:string>review-article</json:string></genre><host><title>Current Opinion in Structural Biology</title><language><json:string>unknown</json:string></language><publicationDate>2000</publicationDate><issn><json:string>0959-440X</json:string></issn><pii><json:string>S0959-440X(00)X0004-8</json:string></pii><volume>10</volume><issue>2</issue><pages><first>242</first><last>250</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>2000</json:string><json:string>13S</json:string><json:string>20S</json:string><json:string>19S</json:string><json:string>26S</json:string><json:string>03/27/2000</json:string></date><geogName></geogName><orgName><json:string>Laboratory of Structural Biology, Building</json:string><json:string>Elsevier Science Ltd.</json:string><json:string>National Institutes of Health, Bethesda, MD</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Andreas Ruepp</json:string><json:string>Sorel Fitz-Gibbon</json:string><json:string>Wolfgang Baumeister</json:string><json:string>In</json:string><json:string>David Belnap</json:string><json:string>Kornelius</json:string><json:string>Alasdair Steven</json:string></persName><placeName><json:string>Specificity</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[83]</json:string><json:string>[4]</json:string><json:string>[43,44]</json:string><json:string>[78]</json:string><json:string>[1,4,59]</json:string><json:string>[82]</json:string><json:string>[66]</json:string><json:string>[86,87]</json:string><json:string>[8]</json:string><json:string>[25,26]</json:string><json:string>[81]</json:string><json:string>[1]</json:string><json:string>[3,6,7]</json:string><json:string>[65]</json:string><json:string>[3]</json:string><json:string>[42]</json:string><json:string>[90,91]</json:string><json:string>[14,65]</json:string><json:string>[5]</json:string><json:string>Zwickl et al.</json:string><json:string>[67,68]</json:string><json:string>[85]</json:string><json:string>[69]</json:string><json:string>[61,62]</json:string><json:string>[59,73]</json:string><json:string>[9]</json:string><json:string>[84]</json:string><json:string>[88,89]</json:string><json:string>[2]</json:string><json:string>[46]</json:string><json:string>[19]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-QCJZB36Q-7</json:string></ark><categories><wos><json:string>1 - 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(a) Model of the 26S proteasome obtained after combining the 3D reconstruction of the 19S regulator (blue) — the lid (distal) and base (proximal) subcomplexes are indicated by different shades of blue — from Drosophila [32••] with the crystal structure of the 20S core (yellow) from Thermoplasma [65]. (b) A model of the ClpAP protease from E. coli derived from the combination of the 3D reconstruction of the ClpAP protease (blue) [71••] with the crystal structure of the ClpP protease (yellow) [64]. The scale bar represents 10 nm.</note><note type="content">Figure 2: Axial view of the ClpAP complex at 29 Å resolution [71••]. ClpP (yellow) has sevenfold symmetry and ClpA (blue) has sixfold symmetry, so that the interactions between pairs of subunits in the two rings are nonequivalent. Their binding is inferred to be dependent on a key interaction (white asterisk) between one specific subunit in ClpA (red dot) and one ClpP subunit (green dot). Relative rotation by only 8.6° (equivalent to a shift of 4.5 Å at the point of contact) transfers the key relationship to neighboring subunits. Thus, the symmetry mismatch is conducive to relative rotation without disengagement of the two subcomplexes. Such rotation might occur during the processive translocation of substrates into ClpP [71••]. A similar symmetry mismatch occurs in the 26S proteasome and some other energy-dependent proteases (see Table 1).</note><note type="content">Table 1: Symmetry in subcomplexes of ATP-dependent proteases</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Dis-assembly lines: the proteasome and related ATPase-assisted proteases</title><author xml:id="author-0000"><persName><forename type="first">Peter</forename><surname>Zwickl</surname></persName><affiliation>Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Wolfgang</forename><surname>Baumeister</surname></persName><email>baumeist@biochem.mpg.de</email><affiliation>Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Alasdair</forename><surname>Steven</surname></persName><affiliation>Laboratory of Structural Biology, Building 6, Room B2-34, Center Drive, MSC-2717, NIAMS, National Institutes of Health, Bethesda, MD 20892-2717, USA</affiliation></author><idno type="istex">6B1F6DADCCD3763AC2C268DDAC9BE90AE1349E67</idno><idno type="ark">ark:/67375/6H6-QCJZB36Q-7</idno><idno type="DOI">10.1016/S0959-440X(00)00075-0</idno><idno type="PII">S0959-440X(00)00075-0</idno></analytic><monogr><title level="j">Current Opinion in Structural Biology</title><title level="j" type="abbrev">COSTBI</title><idno type="pISSN">0959-440X</idno><idno type="PII">S0959-440X(00)X0004-8</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2000"></date><biblScope unit="volume">10</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="242">242</biblScope><biblScope unit="page" to="250">250</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2000</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Self-compartmentalizing proteases, such as the proteasome and several prokaryotic energy-dependent proteases, are designed to act in the crowded environment of the cell. Proteins destined for degradation are recognized and unfolded by regulatory subcomplexes that invariably contain ATPase modules, before being translocated into another subcomplex, the proteolytic core, for degradation. The sequential actions effected on substrates are reflected in the linear arrangement of these subcomplexes; thus, the holocomplexes are organized as molecular disassembly and degradation lines.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Structural biology</term></item><item><term>Biochemistry</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>AAA ATPases</term></item><item><term>ARC</term></item><item><term>ClpAP</term></item><item><term>ClpXP</term></item><item><term>HslVU</term></item><item><term>Lon</term></item><item><term>NSF</term></item><item><term>PAN</term></item><item><term>Proteasome</term></item><item><term>Protein degradation</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2000">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-QCJZB36Q-7/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"><istex:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="rev"><item-info><jid>COSTBI</jid><aid>75</aid><ce:pii>S0959-440X(00)00075-0</ce:pii><ce:doi>10.1016/S0959-440X(00)00075-0</ce:doi><ce:copyright type="full-transfer" year="2000">Elsevier Science Ltd</ce:copyright></item-info><head><ce:dochead><ce:textfn>Review</ce:textfn></ce:dochead><ce:title>Dis-assembly lines: the proteasome and related ATPase-assisted proteases</ce:title><ce:author-group><ce:author><ce:given-name>Peter</ce:given-name><ce:surname>Zwickl</ce:surname><ce:cross-ref refid="AFFA"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Wolfgang</ce:given-name><ce:surname>Baumeister</ce:surname><ce:cross-ref refid="AFFA"><ce:sup>a</ce:sup></ce:cross-ref><ce:e-address>baumeist@biochem.mpg.de</ce:e-address></ce:author><ce:author><ce:given-name>Alasdair</ce:given-name><ce:surname>Steven</ce:surname><ce:cross-ref refid="AFFB"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFFA"><ce:label>a</ce:label><ce:textfn>Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany</ce:textfn></ce:affiliation><ce:affiliation id="AFFB"><ce:label>b</ce:label><ce:textfn>Laboratory of Structural Biology, Building 6, Room B2-34, Center Drive, MSC-2717, NIAMS, National Institutes of Health, Bethesda, MD 20892-2717, USA</ce:textfn></ce:affiliation></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Self-compartmentalizing proteases, such as the proteasome and several prokaryotic energy-dependent proteases, are designed to act in the crowded environment of the cell. Proteins destined for degradation are recognized and unfolded by regulatory subcomplexes that invariably contain ATPase modules, before being translocated into another subcomplex, the proteolytic core, for degradation. The sequential actions effected on substrates are reflected in the linear arrangement of these subcomplexes; thus, the holocomplexes are organized as molecular disassembly and degradation lines.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="idt"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Structural biology</ce:text></ce:keyword><ce:keyword><ce:text>Biochemistry</ce:text></ce:keyword></ce:keywords><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>AAA ATPases</ce:text></ce:keyword><ce:keyword><ce:text>ARC</ce:text></ce:keyword><ce:keyword><ce:text>ClpAP</ce:text></ce:keyword><ce:keyword><ce:text>ClpXP</ce:text></ce:keyword><ce:keyword><ce:text>HslVU</ce:text></ce:keyword><ce:keyword><ce:text>Lon</ce:text></ce:keyword><ce:keyword><ce:text>NSF</ce:text></ce:keyword><ce:keyword><ce:text>PAN</ce:text></ce:keyword><ce:keyword><ce:text>Proteasome</ce:text></ce:keyword><ce:keyword><ce:text>Protein degradation</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Dis-assembly lines: the proteasome and related ATPase-assisted proteases</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Dis-assembly lines: the proteasome and related ATPase-assisted proteases</title></titleInfo><name type="personal"><namePart type="given">Peter</namePart><namePart type="family">Zwickl</namePart><affiliation>Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Wolfgang</namePart><namePart type="family">Baumeister</namePart><affiliation>E-mail: baumeist@biochem.mpg.de</affiliation><affiliation>Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alasdair</namePart><namePart type="family">Steven</namePart><affiliation>Laboratory of Structural Biology, Building 6, Room B2-34, Center Drive, MSC-2717, NIAMS, National Institutes of Health, Bethesda, MD 20892-2717, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="Review article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">2000</dateIssued><copyrightDate encoding="w3cdtf">2000</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Self-compartmentalizing proteases, such as the proteasome and several prokaryotic energy-dependent proteases, are designed to act in the crowded environment of the cell. Proteins destined for degradation are recognized and unfolded by regulatory subcomplexes that invariably contain ATPase modules, before being translocated into another subcomplex, the proteolytic core, for degradation. The sequential actions effected on substrates are reflected in the linear arrangement of these subcomplexes; thus, the holocomplexes are organized as molecular disassembly and degradation lines.</abstract><note type="content">Section title: Review</note><note type="content">Figure 1: A comparison of the structures of the 26S proteasome and the ClpAP protease. (a) Model of the 26S proteasome obtained after combining the 3D reconstruction of the 19S regulator (blue) — the lid (distal) and base (proximal) subcomplexes are indicated by different shades of blue — from Drosophila [32••] with the crystal structure of the 20S core (yellow) from Thermoplasma [65]. (b) A model of the ClpAP protease from E. coli derived from the combination of the 3D reconstruction of the ClpAP protease (blue) [71••] with the crystal structure of the ClpP protease (yellow) [64]. The scale bar represents 10 nm.</note><note type="content">Figure 2: Axial view of the ClpAP complex at 29 Å resolution [71••]. ClpP (yellow) has sevenfold symmetry and ClpA (blue) has sixfold symmetry, so that the interactions between pairs of subunits in the two rings are nonequivalent. Their binding is inferred to be dependent on a key interaction (white asterisk) between one specific subunit in ClpA (red dot) and one ClpP subunit (green dot). Relative rotation by only 8.6° (equivalent to a shift of 4.5 Å at the point of contact) transfers the key relationship to neighboring subunits. Thus, the symmetry mismatch is conducive to relative rotation without disengagement of the two subcomplexes. Such rotation might occur during the processive translocation of substrates into ClpP [71••]. A similar symmetry mismatch occurs in the 26S proteasome and some other energy-dependent proteases (see Table 1).</note><note type="content">Table 1: Symmetry in subcomplexes of ATP-dependent proteases</note><subject><genre>Keywords</genre><topic>Structural biology</topic><topic>Biochemistry</topic></subject><subject><genre>Keywords</genre><topic>AAA ATPases</topic><topic>ARC</topic><topic>ClpAP</topic><topic>ClpXP</topic><topic>HslVU</topic><topic>Lon</topic><topic>NSF</topic><topic>PAN</topic><topic>Proteasome</topic><topic>Protein degradation</topic></subject><relatedItem type="host"><titleInfo><title>Current Opinion in Structural Biology</title></titleInfo><titleInfo type="abbreviated"><title>COSTBI</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">2000</dateIssued></originInfo><identifier type="ISSN">0959-440X</identifier><identifier type="PII">S0959-440X(00)X0004-8</identifier><part><date>2000</date><detail type="volume"><number>10</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>129</start><end>264</end></extent><extent unit="pages"><start>242</start><end>250</end></extent></part></relatedItem><identifier type="istex">6B1F6DADCCD3763AC2C268DDAC9BE90AE1349E67</identifier><identifier type="ark">ark:/67375/6H6-QCJZB36Q-7</identifier><identifier type="DOI">10.1016/S0959-440X(00)00075-0</identifier><identifier type="PII">S0959-440X(00)00075-0</identifier><accessCondition type="use and reproduction" contentType="copyright">©2000 Elsevier Science Ltd</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource><recordOrigin>Elsevier Science Ltd, ©2000</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-QCJZB36Q-7/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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