Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA

J Bacteriol. 1999 Sep;181(18):5543-50. doi: 10.1128/JB.181.18.5543-5550.1999.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacteria / genetics*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Biological Evolution*
  • DNA Helicases / metabolism*
  • DNA, Bacterial / chemistry
  • DNA, Bacterial / genetics*
  • DNA, Bacterial / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Endodeoxyribonucleases / chemistry
  • Endodeoxyribonucleases / metabolism*
  • Escherichia coli Proteins*
  • Evolution, Molecular
  • Holliday Junction Resolvases*
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Phylogeny
  • Protein Conformation
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • RuvB protein, Bacteria
  • ruvC protein, E coli
  • RecG protein, E coli
  • Endodeoxyribonucleases
  • Holliday Junction Resolvases
  • RusA protein, E coli
  • Holliday junction DNA helicase, E coli
  • DNA Helicases