Visualization of liquid-liquid phase transitions using a tiny G-quadruplex binding protein

Bikash R. Sahoo, Xiexiong Deng, Ee Lin Wong, Nathan Clark, Harry J. Yang, Alexey Kovalenko, Vivekanandan Subramanian, Bryan B. Guzman, Sarah E. Harris, Budheswar Dehury, Emi Miyashita, J. Damon Hoff, Vojč Kocman, Hirohide Saito, Daniel Dominguez, Janez Plavec and James C. A. Bardwell ()
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Bikash R. Sahoo: University of Michigan
Xiexiong Deng: University of Michigan
Ee Lin Wong: University of Michigan
Nathan Clark: University of Michigan
Harry J. Yang: University of Michigan
Alexey Kovalenko: University of Michigan
Vivekanandan Subramanian: University of Kentucky
Bryan B. Guzman: University of North Carolina
Sarah E. Harris: University of North Carolina
Budheswar Dehury: Manipal School of Life Sciences, Manipal Academy of Higher Education
Emi Miyashita: Kyoto University
J. Damon Hoff: University of Michigan
Vojč Kocman: National Institute of Chemistry
Hirohide Saito: Kyoto University
Daniel Dominguez: University of North Carolina
Janez Plavec: National Institute of Chemistry
James C. A. Bardwell: University of Michigan

Nature Communications, 2025, vol. 16, issue 1, 1-22

Abstract: Abstract Liquid-liquid phase transitions govern a wide range of protein-protein and protein-RNA interactions. Although the importance of multivalency and protein disorder in driving these transitions is clear, there is limited knowledge concerning the structural basis of phase transitions or the conformational changes that accompany this process. In this work, we found that a small human protein, SERF2, is important for the formation of stress granules. We determined the solution NMR structure ensemble of SERF2. We show that SERF2 specifically interacts with non-canonical tetrahelical RNA structures called G-quadruplexes, structures linked to stress granule formation. The biophysical amenability of both SERF2 and RNA G4 quadruplexes have allowed us to characterize the multivalent protein-RNA interactions involved in liquid-liquid phase transitions, the role that protein disorder plays in these transitions, identify the specific contacts involved, and describe how these interactions impact the structural dynamics of the components enabling a detailed understanding of the structural transitions involved in early stages of ribonucleoprotein condensate formation.

Date: 2025
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DOI: 10.1038/s41467-025-63597-7

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