Dis-assembly lines: the proteasome and related ATPase-assisted proteases
Identifieur interne : 003660 ( Main/Exploration ); précédent : 003659; suivant : 003661Dis-assembly lines: the proteasome and related ATPase-assisted proteases
Auteurs : Peter Zwickl [Allemagne] ; Wolfgang Baumeister [Allemagne] ; Alasdair Steven [États-Unis]Source :
- 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
Affiliations:
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Biology, Building 6, Room B2-34, Center Drive, MSC-2717, NIAMS, National Institutes of Health, Bethesda, MD 20892-2717</wicri:regionArea><wicri:noRegion>MD 20892-2717</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Current Opinion in Structural Biology</title><title level="j" type="abbrev">COSTBI</title><idno type="ISSN">0959-440X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2000">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><idno type="ISSN">0959-440X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0959-440X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Acidophilum</term><term>Active sites</term><term>Atpase</term><term>Atpase 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zwickl</term><term>Proteasomal</term><term>Proteasomal atpases</term><term>Proteasome</term><term>Proteasomes</term><term>Protein breakdown</term><term>Protein degradation</term><term>Protein substrates</term><term>Proteolysis</term><term>Proteolytic</term><term>Regulator</term><term>Relative rotation</term><term>Sensitive factor</term><term>Steven</term><term>Struct biol</term><term>Structural organization</term><term>Subcomplex</term><term>Subcomplexes</term><term>Substrate binding</term><term>Substrate proteins</term><term>Subunit</term><term>Subunit composition</term><term>Symmetry mismatch</term><term>Thermoplasma</term><term>Thermoplasma acidophilum</term><term>Translocation</term><term>Type subunits</term><term>Yeast</term><term>Yeast proteasomes</term><term>Zwickl</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml: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.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>États-Unis</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Zwickl, Peter" sort="Zwickl, Peter" uniqKey="Zwickl P" first="Peter" last="Zwickl">Peter Zwickl</name></noRegion><name sortKey="Baumeister, Wolfgang" sort="Baumeister, Wolfgang" uniqKey="Baumeister W" first="Wolfgang" last="Baumeister">Wolfgang Baumeister</name><name sortKey="Baumeister, Wolfgang" sort="Baumeister, Wolfgang" uniqKey="Baumeister W" first="Wolfgang" last="Baumeister">Wolfgang Baumeister</name></country><country name="États-Unis"><noRegion><name sortKey="Steven, Alasdair" sort="Steven, Alasdair" uniqKey="Steven A" first="Alasdair" last="Steven">Alasdair Steven</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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