Nucleotide excision repair at the single-molecule level : analysis of the E. coli UvrA protein

Abstract

In this thesis, the characteristics of the Escherichia coli UvrA protein were analyzed with microscopy techniques that allow detection of protein complexes at the single-molecule level. Together with UvrB and UvrC, UvrA catalyzes the excision of damaged DNA from the bacterial genome. This DNA repair mechanism is called Nucleotide Excision Repair (NER) and is also conserved in higher organisms. In the current model for bacterial NER, DNA repair is initiated by a complex of two UvrA and two UvrB subunits, the A2B2-complex. In this complex, the two UvrA subunits probe the genome for potential lesions. The mechanism of DNA damage recognition by UvrA is further revealed in this thesis.