Abstract
Different classes of DNA repair systems exist to counteract the effect of the many forms of DNA damage that are generated by exposure of living cells to ultraviolet or ionising radiation and a variety of chemicals. Of these repair systems the nucleotide excision repair pathway is unique in its ability to recognise and repair a vast array of structurally unrelated DNA lesions (see Van Houten 1990 for review). The principles of nucleotide excision repair are the same in prokaryotic and eukaryotic organisms. After recognition of a DNA lesion, incisions are made in the damaged strand on both sides of the lesion, the oligonucleotide containing the lesion is removed, and the resulting gap is filled by DNA synthesis followed by ligation of the remaining nick. The proteins involved in the prokaryotic system, however, differ from those of the eukaryotic system, indicating that the two repair processes are not evolutionaryly related. Whereas eukaryotic nucleotide excision repair requires about 30 polypeptides (Sancar 1996), just 6 proteins (UvrA, UvrB, UvrC, UvrD, DNA polymerase (Pol) I and ligase) are sufficient for carrying out the repair process in E. coli.
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Goosen, N., Moolenaar, G.F., Visse, R., van de Putte, P. (1998). Functional Domains of the E. coli UvrABC Proteins in Nucleotide Excision Repair. In: Eckstein, F., Lilley, D.M.J. (eds) DNA Repair. Nucleic Acids and Molecular Biology, vol 12. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-48770-5_5
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