ArticleJournal of molecular evolution2006
Proteasome-related HslU and HslV genes typical of eubacteria are widespread in eukaryotes.
Article in Journal of molecular evolution, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- ProEnd: a comprehensive database for identifying HbYX motif-containing proteins across the tree of life.BMC genomics · 2024Article
- ProEnd: A Comprehensive Database for Identifying HbYX Motif-Containing Proteins Across the Tree of Life.bioRxiv : the preprint server for biology · 2024Article
- A Transient π-π or Cation-π Interaction between Degron and Degrader Dual Residues: A Key Step for the Substrate Recognition and Discrimination in the Processive Degradation of SulA by ClpYQ (HslUV) Protease inInternational journal of molecular sciences · 2023Article
- The HslV Protease fromInternational journal of molecular sciences · 2019Article
- Insights into the molecular evolution of HslU ATPase through biochemical and mutational analyses.PloS one · 2014Article
- Structural and biochemical analyses of the eukaryotic heat shock locus V (HslV) from Trypanosoma brucei.The Journal of biological chemistry · 2013Article
- Asymmetric nucleotide transactions of the HslUV protease.Journal of molecular biology · 2008Article
- Identification of a bacterial-like HslVU protease in the mitochondria of Trypanosoma brucei and its role in mitochondrial DNA replication.PLoS pathogens · 2008Article
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Many eubacteria contain an ATP-dependent protease complex, which is built by multiple copies of the HslV and HslU proteins and is therefore called HslVU. HslU proteins are AAA + ATPases, while HslV proteins are proteases that show highly significant similarity to beta subunits of proteasomes. Therefore, the HslVU complex has been envisaged as a precursor or ancestral type of proteasome. Here we show that species of most of the main eukaryotic lineages have HslU and HslV genes very similar to those found in proteobacteria. We have detected them in amoebozoa, plantae, chromoalveolata, rhizaria, and excavata species. Phylogenetic analyses suggest that these genes have been obtained by endosymbiosis from the proteobacterial ancestor that gave rise to eukaryotic mitochondria. The products encoded by these eukaryotic genes adopt, according to modeling based on the known crystal structures of prokaryotic HslU and HslV proteins, conformations that are compatible with their being fully active, suggesting that functional HslVU complexes may be present in many eukaryotic species.
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