Disease relevance of recA

• The isolated circle was transferred to Escherichia coli where it integrated specifically into phe tRNA genes, as it does in S. flexneri, independently of recA [1].
• (ii) UV-irradiated phages were recovered by photoreactivation and/or SOS repair mediated by target bacteria and plated on a recA uvrA bacterial lawn in the dark to avoid recovery of noninfecting phages [2].
• The six selected strains were identified as Lactobacillus plantarum by 16S rDNA sequencing, species-specific PCR and multiplex PCR of the recA gene [3].
• Transcriptional analysis of the recA gene of Streptococcus thermophilus [4].
• Two Escherichia coli genes, expressed from multicopy plasmids, are shown to cause partial induction of prophage lambda in recA mutant lysogens [5].

High impact information on recA

• To obtain structural information about the self-association of the protein RecA, we studied urea denaturation of RecA by circular dichroism spectroscopy and gel filtration [6].
• On an adduct basis N-Acetoxy-N-2-acetylaminofluorene was shown to induce the protein RecA at a similar level as U.V. On the other hand, N-hydroxy-N-2-aminofluorene shows only a poor induction capacity of the RecA protein [7].
• We also discovered that recA was expressed at high constitutive levels, due to constitutive LexA cleavage by RecA, with little induction following DNA damage [8].
• Analyses of the Brucella spp. genomes and our molecular studies documented the presence of only one recA gene, suggesting a RecA-independent repair process [8].
• The appearance of Arg(+) mutants on the plates with streptomycin was not significantly altered by recA, rpoS or dps mutations [9].

Biological context of recA

• Interestingly, deletion did not occur in A. tumefaciens strain AGL1 with a recA mutation in C58 chromosome, implying a clear role for recombination in deletion [10].
• A 100-fold reduction in the recombination rate was observed in a recA mutant strain even though crossing-over was still efficient [11].
• In Escherichia coli the LexA protein acts as a recA repressor and is able, in response to DNA damage, of RecA-promoted self-cleavage, thus allowing recA transcription [4].
• The analysis of deletion mutants and of translational gene fusions showed that a DNA region of 83 base pairs, containg the recA promoter and the transcriptional start site, is sufficient to ensure normal expression of the gene [4].
• Base up-regulated core genes for maltodextrin transport (lamB, mal), ATP synthase (atp), and DNA repair (recA, mutL) [12].

Anatomical context of recA

• Using single-stranded DNA, non-coated constructs produced a transgene integration rate of 0.5%, while none of the 1040 zygotes injected with recombinase A-coated constructs produced transgenic pups [13].

Analytical, diagnostic and therapeutic context of recA

• By means of an immunoradiometric assay the induction of protein RecA in E. coli PQ 10 was measured after treatment by two related carcinogens [7].

References