ArticleBiochemistry and biophysics reports2021
Comparative study of His- and Non-His-tagged CLIC proteins, reveals changes in their enzymatic activity.
Article in Biochemistry and biophysics reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- EngineeredSynthetic and systems biotechnology · 2026Article
- CLIC3 is upregulated across all subtypes of breast cancer and plays a key role in cell migration, invasion and growth in soft agar.Breast cancer research : BCR · 2026Article
- Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified bySmall science · 2025Article
- Increasing thermostability of the key photorespiratory enzyme glycerate 3-kinase by structure-based recombination.Plant biotechnology journal · 2025Article
- CLIC1 and CLIC4 demonstrate cell protective antioxidant activity against UV exposure.Frontiers in cell and developmental biology · 2025Article
- Enhanced efficacy of the novel recombinant clone VasSF in a mouse model of antineutrophil cytoplasmic antibody-associated vasculitis.Clinical and experimental immunology · 2024Article
- Article
- Generation of auxin inducible degron (AID) knock-in cell lines for targeted protein degradation in mammalian cells.STAR protocols · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chloride intracellular ion channel protein (CLIC) family are a unique set of ion channels that can exist as soluble and integral membrane proteins. New evidence has emerged that demonstrates CLICs' possess oxidoreductase enzymatic activity and may function as either membrane-spanning ion channels or as globular enzymes. To further characterize the enzymatic profile of members of the CLIC family and to expand our understanding of their functions, we expressed and purified recombinant CLIC1, CLIC3, and a non-functional CLIC1-Cys24A mutant using a Histidine tag, bacterial protein expression system. We demonstrate that the presence of the six-polyhistidine tag at the amino terminus of the proteins led to a decrease in their oxidoreductase enzymatic activity compared to their non-His-tagged counterparts, when assessed using 2-hydroxyethyl disulfide as a substrate. These results strongly suggest the six-polyhistidine tag alters CLIC's structure at the N-terminus, which also contains the enzyme active site. It also raises the need for caution in use of His-tagged proteins when assessing oxidoreductase protein enzymatic function.
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