Insights into the mechanisms of homologous recombination from the structure of RuvA.
The recent structure determination of RuvA has provided the first insights into the structural basis for its interaction with Holliday junction DNA. Multiple copies of a helix-hairpin-helix motif which line the four grooves between the monomers in the tetrameric structure are thought to be involved in the interaction of the protein with its DNA target. This suggests that the four arms of the junction are held by RuvA in a fourfold symmetric arrangement and has fuelled ideas on the way in which components of the Ruv complex combine to catalyse the process of homologous recombination.
Rice
D W
DW
Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK. d.rice@sheffield.ac.uk
Rafferty
J B
JB
Artymiuk
P J
PJ
Lloyd
R G
RG
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D004265:DNA Helicases; D004260:DNA Repair; D004269:DNA, Bacterial / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D004706:Endodeoxyribonucleases / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D029968:Escherichia coli Proteins; D018257:Helix-Loop-Helix Motifs; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D011995:Recombination, Genetic
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C061260:RuvB protein, Bacteria; C069806:ruvC protein, E coli; D004706:Endodeoxyribonucleases; C071059:Holliday junction DNA helicase, E coli; D004265:DNA Helicases