ArticleThe Journal of biological chemistry2013
Pyrococcus horikoshii TET2 peptidase assembling process and associated functional regulation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 ofThe Journal of biological chemistry · 2019Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Characterization of a Glycyl-Specific TET Aminopeptidase Complex from Pyrococcus horikoshii.Journal of bacteriology · 2018Article
- Unraveling self-assembly pathways of the 468-kDa proteolytic machine TET2.Science advances · 2017Article
- Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites.Scientific reports · 2016Article
- Heat-induced conformational changes of TET peptidase from crenarchaeon Desulfurococcus kamchatkensis.European biophysics journal : EBJ · 2015Article
- Structure of the dodecamer of the aminopeptidase APDkam598 from the archaeon Desulfurococcus kamchatkensis.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase.Acta crystallographica. Section D, Biological crystallography · 2014Article
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tetrahedral (TET) aminopeptidases are large polypeptide destruction machines present in prokaryotes and eukaryotes. Here, the rules governing their assembly into hollow 12-subunit tetrahedrons are addressed by using TET2 from Pyrococcus horikoshii (PhTET2) as a model. Point mutations allowed the capture of a stable, catalytically active precursor. Small angle x-ray scattering revealed that it is a dimer whose architecture in solution is identical to that determined by x-ray crystallography within the fully assembled TET particle. Small angle x-ray scattering also showed that the reconstituted PhTET2 dodecameric particle displayed the same quaternary structure and thermal stability as the wild-type complex. The PhTET2 assembly intermediates were characterized by analytical ultracentrifugation, native gel electrophoresis, and electron microscopy. They revealed that PhTET2 assembling is a highly ordered process in which hexamers represent the main intermediate. Peptide degradation assays demonstrated that oligomerization triggers the activity of the TET enzyme toward large polypeptidic substrates. Fractionation experiments in Pyrococcus and Halobacterium cells revealed that, in vivo, the dimeric precursor co-exists together with assembled TET complexes. Taken together, our observations explain the biological significance of TET oligomerization and suggest the existence of a functional regulation of the dimer-dodecamer equilibrium in vivo.
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