ArticleArchaea (Vancouver, B.C.)2002
Characterization of the proteasome from the extremely halophilic archaeon Haloarcula marismortui.
Article in Archaea (Vancouver, B.C.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins.International journal of molecular sciences · 2023Review
- Experimental study of proteome halophilicity using nanoDSF: a proof of concept.Extremophiles : life under extreme conditions · 2021Article
- Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.The EMBO journal · 2016Article
- Molecular adaptation and salt stress response of Halobacterium salinarum cells revealed by neutron spectroscopy.Extremophiles : life under extreme conditions · 2015Article
- Production and Characterization of α-Amylase from an Extremely Halophilic Archaeon,Food technology and biotechnology · 2015Article
- Stress regulation of the PAN-proteasome system in the extreme halophilic archaeon Halobacterium.Extremophiles : life under extreme conditions · 2012Article
- Utilization of vinasse for the production of polyhydroxybutyrate by Haloarcula marismortui.Folia microbiologica · 2012Article
- Role of the beta1 subunit in the function and stability of the 20S proteasome in the hyperthermophilic archaeon Pyrococcus furiosus.Journal of bacteriology · 2007Article
- Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii.Journal of bacteriology · 2006Article
- Subunit topology of two 20S proteasomes from Haloferax volcanii.Journal of bacteriology · 2003Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 20S proteasome, comprising two subunits alpha and beta, was purified from the extreme halophilic archaeon Haloarcula marismortui, which grows only in saturated salt conditions. The three-dimensional reconstruction of the H. marismortui proteasome (Hm proteasome), obtained from negatively stained electron micrographs, is virtually identical to the structure of a thermophilic proteasome filtered to the same resolution. The stability of the Hm proteasome was found to be less salt-dependent than that of other halophilic enzymes previously described. The proteolytic activity of the Hm proteasome was investigated using the malate dehydrogenase from H. marismortui (HmMalDH) as a model substrate. The HmMalDH denatures when the salt concentration is decreased below 2 M. Under these conditions, the proteasome efficiently cleaves HmMalDH during its denaturation process, but the fully denatured HmMalDH is poorly degraded. These in vitro experiments show that, at low salt concentrations, the 20S proteasome from halophilic archaea eliminates a misfolded protein.
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