Related Experiment Video
Updated: Sep 25, 2026

Synthetic Condensates and Cell-Like Architectures from Amphiphilic DNA Nanostructures
Published on: May 31, 2024
Selective engineering of condensation properties of single-stranded DNA binding (SSB) protein via its intrinsically
Péter Ecsédi1, Dávid Érfalvy1, Zoltán J Kovács1,2
1ELTE-MTA "Momentum" Motor Enzymology Research Group, De partment of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117 Budapest, Hungary.
Abstract:
Single-stranded DNA binding (SSB) proteins are essential components of genome metabolism in both bacteria and eukaryotes. Recently demonstrated condensation propensities have placed SSB functions in a new context regarding the organization of nucleic acid-modifying complexes. In this work, we provide functional dissection of the condensation and partner binding properties of Escherichia coli (Ec) SSB via engineered modifications of its intrinsically disordered linker (IDL) region. We identify specific alterations in two glycine-rich regions as well as aromatic and/or positively charged residues of the IDL by which a broad-range, selective modification of condensation propensity and condensate thermal and chemical stability can be achieved, while leaving the single-stranded DNA and partner protein binding functions of SSB unchanged. AlphaFold 3-predicted structures of tetrameric wild-type and engineered EcSSB constructs identify multiple possible binding sites for the conserved C-terminal tip on the tetramer core of the IDL, establishing a link between condensation propensity and restrictions in IDL conformational dynamics. Besides defining the contributions of IDL-driven interactions to driving protein condensation, these results pave the way for the definition of in vivo roles of EcSSB condensation via genetic engineering and delineate ways for further development of liquid-liquid phase separation prediction algorithms.
Related Concept Videos
Single-Strand DNA Binding Proteins
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Fixing Double-strand Breaks
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
