Contrasting roles of DBHS disordered regions on liquid phase behaviour and subnuclear organisation

Research output: Contribution to conferenceConference presentation/ephemera


The huge diversity of stable folded structures formed by proteins with complex amino acid sequences has been well characterised and can be confidently predicted. A large proportion of proteins, however, contain regions enriched in only a few amino acids - low-complexity regions (LCRs) - commonly predicted to be intrinsically disordered. Relationships between the amino acid composition of LCRs, protein structure, material behaviour and function are poorly understood. DBHS proteins are RNA-binding proteins that are particularly abundant in the mammalian cell nucleus, involved in transcription, RNA-processing and formation of membraneless organelles. While DBHS proteins have a highly conserved core folded dimerisation domain, their extended LCRs at each terminus are highly diverse, providing a unique opportunity for determining composition-function relationships of LCRs. We have shown that the LCRs of these proteins are central to their ability to functionally aggregate via a process called liquid-liquid phase separation, driving the dynamic, reversible organisation of molecules in the nucleus. Using various in vitro biophysical assays combined with protein localisation studies in cell culture, we aim to understand how amino acid composition of these LCRs determines protein material state and function. Importantly, our work indicates that the phase behaviour conferred by a given LCR on a protein is context-dependent, that is, dependent on the composition of other regions present in the protein.
Original languageEnglish
Publication statusPublished - 2022
EventComBio2022 - Melbourne Convention and Exhibition Centre (MCEC), Melbourne, Australia
Duration: 27 Sept 202230 Sept 2022


Internet address


Dive into the research topics of 'Contrasting roles of DBHS disordered regions on liquid phase behaviour and subnuclear organisation'. Together they form a unique fingerprint.

Cite this