A mechanism for MEX-5-driven disassembly of PGL-3/RNA condensates in vitro.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 40354522.
- Also identified by DOI 10.1073/pnas.2412218122 and PMC identifier 12107180.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
MEX-5 regulates the formation and dissolution of P granules in <i>Caenorhabditis elegans</i> embryos, yet the thermodynamic basis of its activity remains unclear. Here, using a time-resolved in vitro reconstitution system, we show that MEX-5 dissolves preassembled liquid-like PGL-3/RNA condensates by altering RNA availability and shifting the phase boundary. We develop a microfluidic assay to systematically analyze how MEX-5 influences phase separation. By measuring the contribution of PGL-3 to phase separation, we show that MEX-5 reduces the free energy of PGL-3, shifting the equilibrium toward dissolution. Our findings provide a quantitative framework for understanding how RNA-binding proteins modulate condensate stability and demonstrate the power of microfluidics in precisely mapping phase transitions.
Medical subject headings
- Caenorhabditis elegans
- RNA-Binding Proteins
- Caenorhabditis elegans Proteins
- RNA
- RNA, Helminth
- Biomolecular Condensates