Skip to Main content Skip to Navigation
Journal articles

Molecular principles of recruitment and dynamics of guest proteins in liquid droplets

Abstract : Despite the continuous discovery of host and guest proteins in membraneless organelles, complex host–guest interactions hinder the understanding of the molecular grammar governing liquid–liquid phase separation. In this study, we characterized the localization and dynamic properties of guest proteins in liquid droplets using single-molecule fluorescence microscopy. Eighteen guest proteins of different sizes, structures, and oligomeric states were examined in host p53 liquid droplets. Recruitment did not significantly depend on the structural properties of the guest proteins, but was moderately correlated with their length, total charge, and number of R and Y residues. In contrast, the diffusion of disordered guest proteins was comparable to that of host p53, whereas that of folded proteins varied widely. Molecular dynamics simulations suggest that folded proteins diffuse within the voids of the liquid droplet while interacting weakly with neighboring host proteins, whereas disordered proteins adapt their structures to form tight interactions with the host proteins. Our study provides insights into the key molecular principles of the localization and dynamics of guest proteins in liquid droplets.
Document type :
Journal articles
Complete list of metadata
Contributor : Isabelle Frapart Connect in order to contact the contributor
Submitted on : Friday, November 19, 2021 - 11:24:31 AM
Last modification on : Friday, April 1, 2022 - 3:55:44 AM
Long-term archiving on: : Sunday, February 20, 2022 - 6:41:51 PM


Publisher files allowed on an open archive




Kiyoto Kamagata, Nanako Iwaki, Milan Kumar Hazra, Saori Kanbayashi, Trishit Banerjee, et al.. Molecular principles of recruitment and dynamics of guest proteins in liquid droplets. Scientific Reports, Nature Publishing Group, 2021, 11 (1), ⟨10.1038/s41598-021-98955-0⟩. ⟨hal-03433608⟩



Record views


Files downloads