Structural and functional characterization of a hyperthermostable single‐stranded DNA ‐binding protein from a hot spring metagenome

Researchers have identified and characterized a hyperthermostable single-stranded DNA-binding protein (SSB-M5) from a hot spring metagenome in Vatnajökull National Park, Iceland. This small protein, derived from hyperthermophilic Fervidobacterium species, demonstrates remarkable stability and high affinity for single-stranded DNA, even at temperatures up to 100°C. Structural analysis revealed that SSB-M5 forms a tetrameric functional unit, while biochemical assays confirmed its ability to substitute for Escherichia coli SSB in mutant strains. Notably, SSB-M5 exhibits cooperative binding with an EC50 of 141 pM and a Hill coefficient of 2, indicating strong and specific interactions with DNA. Its inclusion in PCR reactions significantly enhances amplification by eliminating non-specific products, highlighting its potential applications in molecular biology and biotechnology.

Werbowy, O., Håkansson, M., Dorawa, S., Stefańska‐Kaźmierczak, A., Svensson, L. A., Al‐Karadaghi, S., Jurczak‐Kurek, A., Kwiatkowska‐Semrau, K., Plotka, M., Fridjonsson, O. H., Hreggvidsson, G. O., Aevarsson, A., Dąbrowski, S., Kaczorowska, A.-K., & Kaczorowski, T. (2026). Structural and functional characterization of a hyperthermostable single‐stranded DNA ‐binding protein from a hot spring metagenome. Protein Science, 35(4). Portico. https://doi.org/10.1002/pro.70538