ArticleAntioxidants (Basel, Switzerland)2023
The Molecular Chaperone Mechanism of the C-Terminal Domain of Large-Size Subunit Catalases.
Article in Antioxidants (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 2 citations in OpenAlex.
- High-Throughput Screening Method UsingMicroorganisms · 2024Article
- Catalase from the Antarctic FungusIndian journal of microbiology · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Large-size subunit catalases (LSCs) have an additional C-terminal domain (CT) that is structurally similar to Hsp31 and DJ-1 proteins, which have molecular chaperone activity. The CT of LSCs derives from a bacterial Hsp31 protein. There are two CT dimers with inverted symmetry in LSCs, one dimer in each pole of the homotetrameric structure. We previously demonstrated the molecular chaperone activity of the CT of LSCs. Like other chaperones, LSCs are abundant proteins that are induced under stress conditions and during cell differentiation in bacteria and fungi. Here, we analyze the mechanism of the CT of LSCs as an unfolding enzyme. The dimeric form of catalase-3 (CAT-3) CT (TDC3) of
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