title: Conservation of eukaryotic DNA repair mechanisms.
abstract: OBJECTIVE
  To discuss the evolutionary conservation of different DNA repair processes. The proteins that carry out base excision repair show a varying degree of structural conservation, but a high level of functional complementation between species, as might be expected for a sequential pathway. In nucleotide excision repair there is a high degree of structural conservation, but few examples of functional complementation because the process involves multiprotein complexes. Repair by homologous recombination involves proteins that are highly conserved structurally. The process of repair of DNA breaks by non-homologous end-joining is conserved in eukaryotes, but the level of sequence identity of several of the proteins is fairly low and some components involved in man do not appear to have sequence homologues in yeast.
  
  
  CONCLUSIONS
  All DNA repair processes are highly conserved. The degree of structural and functional conservation varies between the different processes.
authors.affiliation: MRC Cell Mutation Unit, Sussex University, Falmer, Brighton, UK.
authors.forename: E M
authors.initials: EM
authors.lastname: Taylor
authors.forename: A R
authors.initials: AR
authors.lastname: Lehmann
mesh_terms: D000818:Animals; D034961:Antigens, Nuclear; D019757:Carbon-Oxygen Lyases; D004265:DNA Helicases; D000072481:DNA Ligase ATP; D011088:DNA Ligases; D004260:DNA Repair / Q000235:genetics*; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D004268:DNA-Binding Proteins; D043223:Deoxyribonuclease IV (Phage T4-Induced); D004926:Escherichia coli; D029968:Escherichia coli Proteins; D005057:Eukaryotic Cells; D019143:Evolution, Molecular; D006801:Humans; D000072200:Ku Autoantigen; D009687:Nuclear Proteins; D000075223:Poly-ADP-Ribose Binding Proteins; D016601:RNA-Binding Proteins; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013045:Species Specificity; D035381:TATA-Binding Protein Associated Factors; D035362:Transcription Factor TFIID; D051758:Transcription Factor TFIIH; D014157:Transcription Factors; D019473:Transcription Factors, TFII; D029867:Xenopus Proteins; D051760:Xeroderma Pigmentosum Group A Protein
chemical_list: D034961:Antigens, Nuclear; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D009687:Nuclear Proteins; D000075223:Poly-ADP-Ribose Binding Proteins; D016601:RNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; C490039:TAF6 protein, S cerevisiae; D035381:TATA-Binding Protein Associated Factors; D035362:Transcription Factor TFIID; D014157:Transcription Factors; D019473:Transcription Factors, TFII; C497314:XPA protein, human; C101467:XRCC4 protein, human; D029867:Xenopus Proteins; D051760:Xeroderma Pigmentosum Group A Protein; C081647:high affinity DNA-binding factor, S cerevisiae; D051758:Transcription Factor TFIIH; D043223:Deoxyribonuclease IV (Phage T4-Induced); C468972:endonuclease IV, E coli; D004265:DNA Helicases; C106893:XRCC5 protein, human; C000606509:Xrcc6 protein, human; D019757:Carbon-Oxygen Lyases; D000072200:Ku Autoantigen; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D011088:DNA Ligases; D000072481:DNA Ligase ATP; C000618816:DNA ligase III alpha protein, Xenopus