Convergent evolution of MutS and topoisomerase II for clamping DNA crossovers and stacked Holliday junctions.
This study shows that topoisomerase II and MutS proteins share a structural motif that has, in its dimeric form, a suitable geometry for clamping the two arms of either right-handed DNA crossovers or their isostructural stacked Holliday junctions. This defines a new protein family selected by convergent evolution for sensing DNA topology and binding recombination intermediates. This study also proposes that MutS binding on 2-fold right-handed crossover provides a mechanism for strand discrimination during DNA translocation.
Timsit
Y
Y
Institut de Biologie Physico-Chimique, CNRS, Paris, France. timsit@ibpc.fr
D000251:Adenosine Triphosphatases; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D020137:Base Pair Mismatch; D001665:Binding Sites; D004250:DNA Topoisomerases, Type II / Q000737:chemistry* / Q000235:genetics*; D004269:DNA, Bacterial / Q000737:chemistry*; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D019143:Evolution, Molecular; D008958:Models, Molecular; D051719:MutS DNA Mismatch-Binding Protein; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D013379:Substrate Specificity; D013824:Thermus / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D000251:Adenosine Triphosphatases; D051719:MutS DNA Mismatch-Binding Protein; C497175:MutS protein, E coli; D004250:DNA Topoisomerases, Type II