Co-condensation of proteins with single- and double-stranded DNA

SignificanceBiomolecular 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 dynami...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 119; no. 10; p. e2107871119
Main Authors Renger, Roman, Morin, Jose A, Lemaitre, Regis, Ruer-Gruss, Martine, Jülicher, Frank, Hermann, Andreas, Grill, Stephan W
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 08.03.2022
Subjects
Biological Sciences
Condensates
Condensation
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA, Single-Stranded - chemistry
Force measurement
FUS protein
Humans
Microscopy, Fluorescence
Nuclei (cytology)
Nucleic acids
Phase separation
Polymers
Prion protein
Proteins
RNA-Binding Protein FUS - chemistry
Sarcoma
optical tweezers
FUS
DNA
biomolecular condensates
co-condensation
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Summary:SignificanceBiomolecular 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.
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Author contributions: R.R., J.A.M., A.H., and S.W.G. designed research; R.R. and J.A.M. performed research; R.R., J.A.M., R.L., M.R.-G., and F.J. contributed new reagents/analytic tools; R.R. and S.W.G. analyzed data; and R.R., F.J., A.H., and S.W.G. wrote the paper.
Edited by Rohit Pappu, Biomedical Engineering, Washington University in St. Louis, St. Louis, MO; received April 30, 2021; accepted December 13, 2021 by Editorial Board Member Susan Marqusee
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.2107871119