Proteolytic Processing and Assembly of the C5 Subunit into the Proteasome Complex
Assembly of mammalian 20 S proteasomes from individual subunits is beginning to be investigated. Proteasomes are made of four heptameric rings in the configuration α7β7β7α7. By using anti-proteasome and anti-subunit-specific antibodies, we characterized the processing and assembly of the β subunit C...
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| Veröffentlicht in: | The Journal of biological chemistry 2000-03, Vol.275 (9), p.6592-6599 |
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| container_issue | 9 |
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| container_title | The Journal of biological chemistry |
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| creator | Rodriguez-Vilariño, Susana Arribas, Joaquı́n Arizti, Paz Castaño, José G. |
| description | Assembly of mammalian 20 S proteasomes from individual subunits is beginning to be investigated. Proteasomes are made of four heptameric rings in the configuration α7β7β7α7. By using anti-proteasome and anti-subunit-specific antibodies, we characterized the processing and assembly of the β subunit C5. The C5 precursor (25 kDa) remains as a free non-assembled polypeptide in the cell. The conversion of the C5 precursor to mature C5 (23 kDa) occurs concomitantly with its incorporation into 15 S proteasome intermediate and 20 S mature proteasome complexes. This processing is dependent on proteasome activity and takes place in the cytosol. These results are not fully compatible with the hypothesis that postulates that assembly of proteasomes takes place via a “half-proteasome” intermediate that contains one full α-ring and one full β-ring of unprocessed β subunit precursors. |
| doi_str_mv | 10.1074/jbc.275.9.6592 |
| format | Article |
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Proteasomes are made of four heptameric rings in the configuration α7β7β7α7. By using anti-proteasome and anti-subunit-specific antibodies, we characterized the processing and assembly of the β subunit C5. The C5 precursor (25 kDa) remains as a free non-assembled polypeptide in the cell. The conversion of the C5 precursor to mature C5 (23 kDa) occurs concomitantly with its incorporation into 15 S proteasome intermediate and 20 S mature proteasome complexes. This processing is dependent on proteasome activity and takes place in the cytosol. 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Proteasomes are made of four heptameric rings in the configuration α7β7β7α7. By using anti-proteasome and anti-subunit-specific antibodies, we characterized the processing and assembly of the β subunit C5. The C5 precursor (25 kDa) remains as a free non-assembled polypeptide in the cell. The conversion of the C5 precursor to mature C5 (23 kDa) occurs concomitantly with its incorporation into 15 S proteasome intermediate and 20 S mature proteasome complexes. This processing is dependent on proteasome activity and takes place in the cytosol. 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| ispartof | The Journal of biological chemistry, 2000-03, Vol.275 (9), p.6592-6599 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Antibodies - metabolism Cell Line Centrifugation, Density Gradient Cysteine Endopeptidases - biosynthesis Cysteine Endopeptidases - immunology Cytosol - metabolism Humans Immunoblotting Liver - enzymology Multienzyme Complexes - biosynthesis Multienzyme Complexes - immunology Precipitin Tests Proteasome Endopeptidase Complex Protein Biosynthesis Protein Precursors - metabolism Protein Processing, Post-Translational RNA, Messenger - metabolism |
| title | Proteolytic Processing and Assembly of the C5 Subunit into the Proteasome Complex |
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