Disordered DBHS Regions Drive Droplet Formation

Research output: Contribution to conferenceConference presentation/ephemera


Stable folded 3D structures of proteins are well characterised and can be confidently predicted in most cases. A large proportion of proteins, however, contain regions enriched in a few amino acids – low-complexity regions (LCRs) – which are often intrinsically disordered. How LCR composition relates to protein behaviour and function is poorly understood. DBHS proteins are abundant multifunctional RNA-binding proteins with a conserved core folded domain flanked on either side by long highly diverse LCRs, providing a unique opportunity for describing LCR composition-function relationships. We show that LCRs allow these proteins to reversibly condense to form liquid droplets, driving dynamic and reversible organisation of molecules in the cell nucleus.
Original languageEnglish
Publication statusPublished - 2022
EventPerth Protein Group Annual General Meeting 2022 - Curtin University Business School, Perth, Australia
Duration: 26 Oct 202227 Oct 2022


OtherPerth Protein Group Annual General Meeting 2022
Abbreviated titlePPG2022
Internet address


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