Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA.
Sharples
G J
GJ
Institute of Genetics, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, United Kingdom. gary.sharples@nottingham.ac.uk
Ingleston
S M
SM
Lloyd
R G
RG
D000595:Amino Acid Sequence; D001419:Bacteria / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D005075:Biological Evolution; D004265:DNA Helicases / Q000378:metabolism*; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D004706:Endodeoxyribonucleases / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins; D019143:Evolution, Molecular; D045565:Holliday Junction Resolvases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D011487:Protein Conformation; D016415:Sequence Alignment
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C061260:RuvB protein, Bacteria; C069806:ruvC protein, E coli; C071446:RecG protein, E coli; D004706:Endodeoxyribonucleases; D045565:Holliday Junction Resolvases; C112057:RusA protein, E coli; C071059:Holliday junction DNA helicase, E coli; D004265:DNA Helicases