Evolution of proteasomal ATPases
In eukaryotic cells, the majority of proteins are degraded via the ATP-dependent ubiquitin/26S proteasome pathway. The proteasome is the proteolytic component of the pathway. It is a very large complex with a mass of around 2.5 MDa, consisting of at least 62 proteins encoded by 31 genes. The eukaryo...
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| Veröffentlicht in: | Molecular biology and evolution 2001-06, Vol.18 (6), p.962-974 |
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| creator | Wollenberg, K Swaffield, J C |
| description | In eukaryotic cells, the majority of proteins are degraded via the ATP-dependent ubiquitin/26S proteasome pathway. The proteasome is the proteolytic component of the pathway. It is a very large complex with a mass of around 2.5 MDa, consisting of at least 62 proteins encoded by 31 genes. The eukaryotic proteasome has evolved from a simpler archaebacterial form, similar in structure but containing only three different peptides. One of these peptides is an ATPase belonging to the AAA (Triple-A) family of ATPASES: Gene duplication and diversification has resulted in six paralogous ATPases being present in the eukaryotic proteasome. While sequence analysis studies clearly show that the six eukaryotic proteasomal ATPases have evolved from the single archaebacterial proteasomal ATPase, the deep node structures of the phylogenetic constructions lack resolution. Incorporating physical data to provide support for alternative phylogenetic hypotheses, we have constructed a model of a possible evolutionary history of the proteasomal ATPASES: |
| doi_str_mv | 10.1093/oxfordjournals.molbev.a003897 |
| format | Article |
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The proteasome is the proteolytic component of the pathway. It is a very large complex with a mass of around 2.5 MDa, consisting of at least 62 proteins encoded by 31 genes. The eukaryotic proteasome has evolved from a simpler archaebacterial form, similar in structure but containing only three different peptides. One of these peptides is an ATPase belonging to the AAA (Triple-A) family of ATPASES: Gene duplication and diversification has resulted in six paralogous ATPases being present in the eukaryotic proteasome. While sequence analysis studies clearly show that the six eukaryotic proteasomal ATPases have evolved from the single archaebacterial proteasomal ATPase, the deep node structures of the phylogenetic constructions lack resolution. 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| language | eng |
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| source | MEDLINE; Oxford Journals Open Access Collection; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Animals Archaea - enzymology Archaea - genetics Cysteine Endopeptidases - genetics Cysteine Endopeptidases - metabolism Eukaryotic Cells - enzymology Eukaryotic Cells - metabolism Evolution, Molecular Humans Models, Genetic Multienzyme Complexes - genetics Multienzyme Complexes - metabolism Peptide Hydrolases - genetics Peptide Hydrolases - metabolism Phylogeny Proteasome Endopeptidase Complex |
| title | Evolution of proteasomal ATPases |
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