title: Prokaryotic nucleotide excision repair.
abstract: Nucleotide excision repair (NER) has allowed bacteria to flourish in many different niches around the globe that inflict harsh environmental damage to their genetic material. NER is remarkable because of its diverse substrate repertoire, which differs greatly in chemical composition and structure. Recent advances in structural biology and single-molecule studies have given great insight into the structure and function of NER components. This ensemble of proteins orchestrates faithful removal of toxic DNA lesions through a multistep process. The damaged nucleotide is recognized by dynamic probing of the DNA structure that is then verified and marked for dual incisions followed by excision of the damage and surrounding nucleotides. The opposite DNA strand serves as a template for repair, which is completed after resynthesis and ligation.
authors: Rudolf-Virchow-Center for Experimental Biomedicine, University of Wuerzburg, 97080 Wuerzburg, Germany. caroline.kisker@virchow.uni-wuerzburg.de
authors: Caroline
authors: C
authors: Kisker
authors: Jochen
authors: J
authors: Kuper
authors: Bennett
authors: B
authors: Van Houten
mesh_terms: D004249:DNA Damage / Q000235:genetics*; D004260:DNA Repair / Q000502:physiology*; D004706:Endodeoxyribonucleases / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000378:metabolism*; D009711:Nucleotides / Q000378:metabolism*; D011387:Prokaryotic Cells / Q000502:physiology*; D011487:Protein Conformation; D014158:Transcription, Genetic / Q000502:physiology
chemical_list: D029968:Escherichia coli Proteins; D046912:Multiprotein Complexes; D009711:Nucleotides; D004706:Endodeoxyribonucleases; C036385:endodeoxyribonuclease uvrABC; C448636:Cho protein, E coli