Abstract
Eukaryotic cells express thousands of protein domains long believed to function in the absence of molecular order. These intrinsically disordered protein (IDP) domains are typified by gibberish-like repeats of only a limited number of amino acids that we refer to as domains of low sequence complexity. A decade ago, it was observed that these low complexity (LC) domains can undergo phase transition out of aqueous solution to form either liquid-like droplets or hydrogels. The self-associative interactions responsible for phase transition involve the formation of specific cross-β structures that are unusual in being labile to dissociation. Here we give evidence that the LC domains of two RNA binding proteins, ataxin-2 and TDP43, form cross-β interactions that specify biologically relevant redox sensors.
Original language | English (US) |
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Pages (from-to) | 111-118 |
Number of pages | 8 |
Journal | Current Opinion in Genetics and Development |
Volume | 67 |
DOIs | |
State | Published - Apr 2021 |
ASJC Scopus subject areas
- Genetics
- Developmental Biology