Disease relevance of recA

• Analyses of the Brucella spp. genomes and our molecular studies documented the presence of only one recA gene, suggesting a RecA-independent repair process [1].
• The SRRz lysis gene cassette from bacteriophage Lambda was cloned downstream of a UV-inducible promoter, the recA promoter or the umuDC promoter, and further inserted into the backbone of pUC18, and transformed into E. coli BL21 cells [2].
• For instance, Pol V, the major lesion bypass polymerase in Escherichia coli, requires a functional interaction with the tip of the RecA filament [3].
• Distinguishing characteristics of hyperrecombinogenic RecA protein from Pseudomonas aeruginosa acting in Escherichia coli [4].
• In vivo assays indicated that Mycobacterium tuberculosis recA partially complemented Escherichia coli recA mutants for recombination and mutagenesis [5].

Psychiatry related information on recA

• We describe that although stochastic alignments across poly(dA) and poly(dT) can lead to sub-optimally annealed duplexes containing ssDNA gaps/overhangs, the same are realigned into an optimal frame by a putative motor activity of RecA [Sen et al. (2000) Biochemistry 39, 10196-10206] [6].

High impact information on recA

• So far, Escherichia coli RecA appears to be unique among its nearly ubiquitous family of homologous proteins in that it possesses a motorlike activity that can couple the branch movement in DNA strand exchange to ATP hydrolysis [7].
• RecA is also a multifunctional protein, serving in different biochemical roles for recombinational processes, SOS induction, and mutagenic lesion bypass [7].
• The bacterial RecA protein and the recombinational DNA repair of stalled replication forks [7].
• In Escherichia coli, at least two groups of proteins, or "recombination machines," can operate independently on broken DNA to produce a 3'-terminated single-stranded DNA filament coated with RecA protein and ready for synapsis with intact homologous DNA [8].
• Protein splicing in the maturation of M. tuberculosis recA protein: a mechanism for tolerating a novel class of intervening sequence [9].

Chemical compound and disease context of recA

• A 3.3-kb DNA fragment of Clostridium acetobutylicum conferred methyl methane sulfonate (MMS), mitomycin C (MC), and UV resistance to recA strains of E. coli when cloned on the pUC19 plasmid [10].
• In UV-irradiated Escherichia coli, predamaged by thymine-amino acid starvation or a UV predose, a large amount of dimers may remain unexcised and may be tolerated by an error-free mechanism, which requires the function of uvr, recA and lexA genes [11].
• Repair-deficient and repair-proficient strains of E. coli K12 were sensitive to nitrofurantoin treatment to varying degrees with the double mutant strain (uvrA 6, recA 13) being most sensitive [12].
• Induction of SOS functions: regulation of proteolytic activity of E. coli RecA protein by interaction with DNA and nucleoside triphosphate [13].
• In the presence of adenosine 5'-[gamma-thio]triphosphate, a nonhydrolyzable analog of ATP, Escherichia coli recA protein extensively unwinds duplex DNA in a reaction that is strongly stimulated by either homologous or heterologous single-stranded DNA [Cunningham, R.P., Shibata, T., DasGupta, C. & Radding, C.M. (1979) Nature (London) 281, 191-195] [14].

Biological context of recA

• A deletion of the ykoV gene encoding the B. subtilis Ku protein in a sbcC mutant strain did not resulted in an increase in sensitivity towards MMC and gamma irradiation, but exacerbated the phenotype of a recN or a recA mutant strain [15].
• After UV-induced DNA damage in Escherichia coli, RecA and several recF pathway proteins are thought to process arrested replication forks and ensure that replication resumes accurately [16].
• RecA is important for recombination, DNA repair, and SOS induction [17].
• We investigated the roles of RecA protein, DNA repair, and SOS regulation in B. abortus [1].
• In Escherichia coli, a relatively low frequency of recombination exchanges (FRE) is predetermined by the activity of RecA protein, as modulated by a complex regulatory program involving both autoregulation and other factors [4].

Anatomical context of recA

• We show that RecA but not RadA was required for survival in macrophages [1].
• Using an inducible recA promoter and the g10-L ribosome-binding site, recombinant non-glycosylated interleukin 4 (IL-4) was expressed as 17% of total cellular protein in Escherichia coli inclusion bodies, as a reduced, inactive 14.5-kDa polypeptide [18].
• RecA binds to linear duplex fd DNA in solutions of 0.01 M Tris (pH 7.5) to yield chains of beads which, in the presence of Mg2+ and ATP, coalesce into smooth filaments with a length of 1.9 micrometers (the length of protein-free fd duplex DNA) and have a fiber diameter of 12 nm [19].
• Eukaryotic cells encode two homologs of Escherichia coli RecA protein, Rad51 and Dmc1, which are required for meiotic recombination [20].
• A homolog of Escherichia coli RecA protein in plastids of higher plants [21].

Associations of recA with chemical compounds

• In total, these results suggested that genistein may reduce SOS-dependent mutagenesis by reducing the interaction of RecA protein with ssDNA [22].
• First, lexA protein can be cleaved in vitro under the same conditions as prevously described for lambda repressor cleavage in a reaction requring both recA protease and ATP or an analogue, adenosine 5'-[lambda-thio]-triphosphate [23].
• Short sequence tracts composed of alternating guanosine and thymidine nucleotide residues poly[d(GT)-d(CA)] carried in a derivative of pBR322 were recombinogenic in a recA host [24].
• Incoming ODNs at least 30 nucleotides long cross-linked to a long homologous duplex DNA in the presence of recA and ATP gamma S. Efficient cross-linkage to the complementary recipient strand of the joint occurred preferentially at guanines positioned 5' relative to the appended chlorambucil group [25].
• The revertion to Met+ was shown to be recA dependent, indicating that homologous plasmid and chromosomal DNA sequences are involved in the integration-excision process [26].

Other interactions of recA

• We present functional analyses that demonstrated that B. abortus RadA complements a radA defect in E. coli but could not act in place of the B. abortus RecA [1].
• For both the recA and umuDC promoters, at 30 degrees C the lysis efficiency was found to be consistent and above 60% as measured using beta-galactosidase as the reporter [2].
• Ultraviolet light induction of recA protein in a recB uvrB mutant of Escherichia coli [27].
• The recombinant H. pylori RecA protein produced in Escherichia coli strain GC6 (recA-) was 38 kDa in size but inactive in DNA repair, whereas the corresponding protein in H. pylori 69A migrated at the greater apparent molecular weight of approx. 40 kDa in SDS-polyacrylamide gels [28].
• The results are interpreted in terms of a revised model in which UmuC protein is envisaged as guiding UmuD' to RecA protein which has recognized and become bound to an appropriate DNA lesion [29].

Analytical, diagnostic and therapeutic context of recA

• The Azotobacter vinelandii recA gene: sequence analysis and regulation of expression [30].
• In vivo inactivation of the Streptococcus mutans recA gene mediated by PCR amplification and cloning of a recA DNA fragment [31].
• Electron microscopy of RecA-coated products revealed only knots and catenanes containing a regular right-handed spiral structure [32].
• The basal level of recA protein in Escherichia coli K-12 was estimated by an immunoradiometric assay; it is approximately equal to 1,200 molecules per wild-type bacteria in midexponential phase of growth, slightly more in an excision-deficient (uvrA) strain, and markedly more in recF mutants [33].
• To understand the molecular basis of gene targeting, we have studied interactions of nucleoprotein filaments comprised of single-stranded DNA and RecA protein with chromatin templates reconstituted from linear duplex DNA and histones [34].

References