Abstract
Double stranded DNA (dsDNA), the repository of genetic information in bacteria, archaea and eukaryotes, exhibits a surprising instability in the intracellular environment; this fragility is exacerbated by exogenous agents, such as ultraviolet radiation. To protect themselves against the severe consequences of DNA damage, cells have evolved at least six distinct DNA repair pathways. Here, we review recent key findings of studies aimed at understanding one of these pathways: bacterial nucleotide excision repair (NER). This pathway operates in two modes: a global genome repair (GGR) pathway and a pathway that closely interfaces with transcription by RNA polymerase called transcription-coupled repair (TCR). Below, we discuss the architecture of key proteins in bacterial NER and recent biochemical, structural and single-molecule studies that shed light on the lesion recognition steps of both the GGR and the TCR sub-pathways. Although a great deal has been learned about both of these sub-pathways, several important questions, including damage discrimination, roles of ATP and the orchestration of protein binding and conformation switching, remain to be addressed.
Highlights
A Peek Inside the Machines of Bacterial NucleotideCitation: Kraithong, T.; Hartley, S.; Jeruzalmi, D.; Pakotiprapha, D. A and Danaya Pakotiprapha 2,3, * Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok 10400, Thailand Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand Doctor of Philosophy Programs in Biochemistry, Biology and Chemistry, The Graduate Center of the City University of New York, New York, NY 10016, USA
Published: 19 January 2021The genetic programs of organisms require robust mechanisms to maintain integrity of information carried in the base sequence of double stranded DNA
Mfd binds to RNA polymerase (RNAP) that is stalled by the lesion, pushes it forward to expose the lesion and recruits the nucleotide excision repair (NER) machinery
Summary
Citation: Kraithong, T.; Hartley, S.; Jeruzalmi, D.; Pakotiprapha, D. A and Danaya Pakotiprapha 2,3, * Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok 10400, Thailand Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand Doctor of Philosophy Programs in Biochemistry, Biology and Chemistry, The Graduate Center of the City University of New York, New York, NY 10016, USA
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