ArticleBioscience reports2012
An archaeal protein evolutionarily conserved in prokaryotes is a zinc-dependent metalloprotease.
Article in Bioscience reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
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- Biosynthesis of the Biphenomycin Family of Potent Antibiotics.Angewandte Chemie (International ed. in English) · 2025Article
- Overexpression ofFrontiers in microbiology · 2021Article
- The Origins of Specificity in the Microcin-Processing Protease TldD/E.Structure (London, England : 1993) · 2017Article
- The Proteome and Lipidome of Thermococcus kodakarensis across the Stationary Phase.Archaea (Vancouver, B.C.) · 2016Article
- A Zinc-Dependent Protease AMZ-tk from a Thermophilic Archaeon is a New Member of the Archaemetzincin Protein Family.Frontiers in microbiology · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A putative protease gene (tldD) was previously identified from studying tolerance of letD encoding the CcdB toxin of a toxin-antidote system of the F plasmid in Escherichia coli. While this gene is evolutionarily conserved in archaea and bacteria, the proteolytic activity of encoded proteins remained to be demonstrated experimentally. Here we studied Sso0660, an archaeal TldD homologue encoded in Sulfolobus solfataricus by overexpression of the recombinant protein and characterization of the purified enzyme. We found that the enzyme is active in degrading azocasein and FITC-BSA substrates. Protease inhibitor studies showed that EDTA and o-phenanthroline, two well-known metalloprotease inhibitors, either abolished completely or strongly inhibited the enzyme activity, and flame spectrometric analysis showed that a zinc ion is a cofactor of the protease. Furthermore, the protein forms disulfide bond via the Cys416 residue, yielding protein dimer that is the active form of the enzyme. These results establish for the first time that tidD genes encode zinc-containing proteases, classifying them as a family in the metalloprotease class.
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