The RecA Protein: Structure and Functio

Saccharomyces cerevisiae recA homologues RAD51 and DMC1 have both distinct and overlapping roles in meiotic recombination

“…A recA mutation completely abolishes both conjugational recombination and damage-provoked recombinational repair (Clark & Margulies 1966;Howard-Flanders & Theriot 1966;Roca & Cox 1991). At the biochemical level, RecA protein catalyses the invasion of duplex DNA by a homologous single DNA strand.…”

Role of heteroduplex joints in the functional interactions between human Rad51 and wild-type p53

“…In mitotically growing cells recombination processes are frequently associated with DNA replication in order to allow the bypass of unrepaired lesions, and to repair double-strand breaks (DSBs) generated at replication forks passing a single-strand break (Cox, 1997;Haber, 1999). Due to this vital function of recombination processes during the normal life cycle of cells, the lack of the central enzyme function causes high mortality rates in E. coli devoid of RecA (Roca and Cox, 1990), an early embryonic lethal phenotype of mice nullizygous for rad51 (Lim and Hasty, 1996;Tsuzuki et al, 1996), or results in an extreme sensitivity towards ionizing radiation and methyl methanesulfonate (MMS), as observed with S. cerevisiae cells carrying mutations in rad51 (Game and Mortimer, 1974;Shinohara et al, 1992).…”

“…In E. coli RecA is su cient to exert ATP-dependent homologous pairing and strand exchange over a distance of 6 kb (Roca and Cox, 1990;Kowalczykowski, 1991;Radding, 1991;West, 1992). The eukaryotic counterpart of RecA, the Rad51 protein, was biochemically characterized both from yeast (Sung and Robberson, 1995) and from man (Baumann et al, 1996;Gupta et al, 1997Gupta et al, , 1999aBaumann and West, 1999).…”

The RecA protein as a model molecule for molecular systematic studies of bacteria: Comparison of trees of RecAs and 16S rRNAs from the same species

“…It has been 30 years since the isolation of the first recA mutants in E. coli (Clark and Margulies 1965) and 15 years since the sequencing of the corresponding recA gene (Sancar et al 1980;Horii et al 1980). In that time, studies of the wild type and mutant RecA proteins and genes have yielded a great deal of information about the structure-function relationships of the protein, as well as about the general mechanisms of homologous recombination (Clark and Sandler 1994, Kowalczykowski 1991, Roca and Cox 1990. Such studies have been facilitated greatly by the publication of the crystal structure of the E. coli RecA protein alone, and bound to ADP .…”

“…Partial open reading frames are available from many additional bacterial species. The high levels of sequence similarity, even between proteins from distantly related taxa, and the demonstration that many of the functions and activities of the E. coli RecA are conserved in many of these other proteins (Angov and Camerini-Otero 1994, Gutman et al 1994, Roca and Cox 1990, Wetmur et al 1994, suggest that these proteins are homologs of the E. coli RecA.…”