Shedding Light on DNA-Protein Interactions involved in the Nucleotide Excision Repair pathway - Chapter III - SSBs (thesis data)

Data which allowed for the creation of the figures of the chapter III of the thesis.
Abstract: S
Ingle-strand DNA is prone to damage as well as re-complementation. Organisms have evolved ways to protect single-strand DNA and prevent double-strand DNA to reform using proteins which specifically bind to single-strand DNA/RNA sequences. Generally, one ubiquitous protein exists in a given organism, in Humans, this protein is replication protein A or RPA. The minimal single strand DNA binding domain, oligonucleotide/oligosaccharide binding domain or OB domain or OB fold is conserved throughout evolution, human RPA contains 5 OB domains.
In contrast, archaeal SSBs are usually monomeric and contain a single OB fold. The DNA interaction of SSB from Sulfolobus Solfataricus (SsoSSB) has been previously investigated in our group. In this chapter, we will expand our understanding of two archaeal SSBs: the previously mentioned SSoSSB and Sulfolobus acidocaldarius (SacSSB). We carried out a comparative analysis of their binding properties as a function of ionic strength, temperature and pH. The ability of both proteins to interact with ssDNA (or ssRNA) at extreme conditions make them an interesting tool for some biological applications. In an attempt to modulate the DNA-binding properties of SSBs, we have designed and characterized a chimeric SSB that fuses two OB-folds from solfataricus and acidocaldarius. We showed that this chimeric form improves the binding in every condition tested compared to both single OB fold proteins.
The data files are embargoed until 04/02/2025