Skip to content
2000
Volume 5, Issue 2
  • ISSN: 1389-2037
  • E-ISSN: 1875-5550

Abstract

The bacterial RecA protein has been a model system for understanding how a protein can catalyze homologous genetic recombination. RecA-like proteins have now been characterized from many organisms, from bacteriophage to humans. Some of the RecA-like proteins, including human RAD51, appear to function as helical filaments formed on DNA. However, we currently have high resolution structures of inactive forms of the protein, and low resolution structures of the active complexes formed by RecA-like proteins on DNA in the presence of ATP or ATP analogs. Within a crystal of the E. coli RecA protein, a helical polymer exists, and it has been widely assumed that this polymer is quite similar to the active helical filament formed on DNA. Recent developments have suggested that this may not be the case.

Loading

Article metrics loading...

/content/journals/cpps/10.2174/1389203043486883
2004-04-01
2025-09-01
Loading full text...

Full text loading...

/content/journals/cpps/10.2174/1389203043486883
Loading

  • Article Type:
    Review Article
Keyword(s): genetic recombination; reca protein; reca-dna filament?; reca-like proteins
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test