Open AccessCo-condensation of proteins with single- and double-stranded DNA
Author(s) -
Roman Renger,
José A. Morín,
Regis Lemaitre,
Martine Ruer,
Frank Jülicher,
Andreas Hermann,
Stephan W. Grill
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2107871119
Subject(s) - nucleic acid , dna , biophysics , organelle , chemistry , monolayer , intracellular , fluorescence microscope , nucleic acid thermodynamics , fluorescence , biochemistry , biology , base sequence , physics , quantum mechanics
Significance Biomolecular condensates are intracellular organelles that are not bounded by membranes and often show liquid-like, dynamic material properties. They typically contain various types of proteins and nucleic acids. How the interaction of proteins and nucleic acids finally results in dynamic condensates is not fully understood. Here we use optical tweezers and fluorescence microscopy to study how the prototypical prion-like protein Fused-in-Sarcoma (FUS) condenses with individual molecules of single- and double-stranded DNA. We find that FUS adsorbs on DNA in a monolayer and hence generates an effectively sticky FUS–DNA polymer that collapses and finally forms a dynamic, reversible FUS–DNA co-condensate. We speculate that protein monolayer-based protein–nucleic acid co-condensation is a general mechanism for forming intracellular membraneless organelles.