Correlation Engine 2.0
Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

The structure-driven assembly of multimeric protein complexes and the formation of intracellular phase-like protein condensates have been the subject of intense research. However, the assembly of larger superstructures comprising cellular components such as protein nanoparticles driven by general physical rather than specific biochemical interactions remain relatively uncharacterized. Here, we use gas vesicles (GVs) - genetically encoded protein nanoparticles that form ordered intracellular clusters - as a model system to study the forces driving multi-particle assembly under cytoplasm-like conditions. Our calculations and experimental results show that the ordered assembly of GVs can be achieved by screening their mutual electrostatic repulsion with electrolytes and creating a crowding force with dissolved macromolecules. The precise balance of these forces results in different packing configurations. Biomacromolecules such as polylysine and DNA are capable of driving GV clustering. These results provide basic insights into how physically driven interactions affect the formation of protein superstructures, offer guidance for manipulating nanoparticle assembly in cellular environments through synthetic biology methods, and inform research on the biotechnology applications of GVs. Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved.

Citation

Yuxing Yao, Zhiyang Jin, Bill Ling, Dina Malounda, Mikhail G Shapiro. Self-assembly of protein superstructures by physical interactions under cytoplasm-like conditions. Biophysical journal. 2021 May 19


PMID: 34022233

View Full Text