Zinc finger domains bind low-complexity domain polymers.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 41102184.
- Also identified by DOI 10.1038/s41467-025-64382-2 and PMC identifier 12531337.
- Licence recorded as CC BY-NC-ND.
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Abstract
Self-association of low-complexity protein sequences (LC domains) is important for polymer formation. Several molecular chaperones are involved in the regulation of LC domain polymer formation. However, the mechanisms underlying cell recognition of LC domain polymers remain unclear. Here we show that zinc finger domains (ZnFs) bind LC domains of RNA-binding proteins in a cross-β polymer-dependent manner. ZnFs bound to LC domain hydrogels and suppressed LC domain polymer formation. Moreover, ZnFs preferentially recognize LC domains in the polymeric state. These findings suggest that ZnFs act as physiological regulators of LC domain polymer formation.
Medical subject headings
- Zinc Fingers
- Polymers
- RNA-Binding Proteins