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
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<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>
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<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>
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<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>
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<item><term>AAA ATPases</term>
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<item><term>ARC</term>
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<item><term>ClpAP</term>
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<item><term>ClpXP</term>
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<item><term>Lon</term>
</item>
<item><term>NSF</term>
</item>
<item><term>PAN</term>
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<item><term>Proteasome</term>
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<item><term>Protein degradation</term>
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<ce:title>Dis-assembly lines: the proteasome and related ATPase-assisted proteases</ce:title>
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<ce:textfn>Department of Molecular Structural Biology, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany</ce:textfn>
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<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>
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<ce:keyword><ce:text>AAA ATPases</ce:text>
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<ce:keyword><ce:text>ClpAP</ce:text>
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<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>
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<topic>Biochemistry</topic>
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