Redox-mediated regulation of low complexity domain self-association.
Curr Opin Genet Dev
; 67: 111-118, 2021 04.
Article
in En
| MEDLINE
| ID: mdl-33454579
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-ß 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-ß interactions that specify biologically relevant redox sensors.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
RNA-Binding Proteins
/
DNA-Binding Proteins
/
Ataxin-2
/
Protein Domains
Type of study:
Risk_factors_studies
Language:
En
Journal:
Curr Opin Genet Dev
Journal subject:
GENETICA
Year:
2021
Document type:
Article
Affiliation country:
Japan