ArticleProtein science : a publication of the Protein Society2013
Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 6 citations in OpenAlex.
- Effects of ionic strength on the folding and stability of SAMP1, a ubiquitin-like halophilic protein.Biophysical journal · 2022Article
- Mechanism of salt-induced activity enhancement of a marine-derived laccase, Lac15.European biophysics journal : EBJ · 2018Article
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- Prokaryotic ubiquitin-like protein modification.Annual review of microbiology · 2014Review
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8 authors at 4 institutions in 2 countries.
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Abstract
Eukaryotic ubiquitin and ubiquitin-like systems play crucial roles in various cellular biological processes. In this work, we determined the solution structure of SAMP1 from Haloferax volcanii by NMR spectroscopy. Under low ionic conditions, SAMP1 presented two distinct conformations, one folded β-grasp and the other disordered. Interestingly, SAMP1 underwent a conformational conversion from disorder to order with ion concentration increasing, indicating that the ordered conformation is the functional form of SAMP1 under the physiological condition of H. volcanii. Furthermore, SAMP1 could interact with proteasome-activating nucleotidase B, supposing a potential role of SAMP1 in the protein degradation pathway mediated by proteasome.
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