Evolution of sequence specificity in a restriction endonuclease by a point mutation

Proc Natl Acad Sci U S A. 2008 Jul 29;105(30):10344-7. doi: 10.1073/pnas.0804974105. Epub 2008 Jul 22.

Abstract

Restriction endonucleases (REases) protect bacteria from invading foreign DNAs and are endowed with exquisite sequence specificity. REases have originated from the ancestral proteins and evolved new sequence specificities by genetic recombination, gene duplication, replication slippage, and transpositional events. They are also speculated to have evolved from nonspecific endonucleases, attaining a high degree of sequence specificity through point mutations. We describe here an example of generation of exquisitely site-specific REase from a highly-promiscuous one by a single point mutation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • DNA / chemistry
  • DNA Restriction Enzymes / genetics*
  • Deoxyribonucleases, Type II Site-Specific / genetics*
  • Deoxyribonucleases, Type II Site-Specific / metabolism
  • Ions
  • Kinetics
  • Magnesium / chemistry
  • Metals / chemistry
  • Mutagenesis, Site-Directed
  • Mutation
  • Plasmids / metabolism
  • Point Mutation*
  • Polymerase Chain Reaction
  • Recombination, Genetic

Substances

  • Ions
  • Metals
  • DNA
  • DNA Restriction Enzymes
  • Deoxyribonucleases, Type II Site-Specific
  • GGTACC-specific type II deoxyribonucleases
  • Magnesium