Disease relevance of rsvA

• We studied the dynamics of site-specific recombination by the resolvase encoded by the Escherichia coli transposon Tn3 [1].
• We obtained identical results for the decatenation of the products of two different site-specific recombination enzymes, phage lambda integrase and transposon Tn3 resolvase [2].
• The resolvase partially complements the UV and hydroxyurea hypersensitivity and associated aberrant mitoses of an rqh1(-) mutant [3].
• The broad-host-range plasmid pAM beta 1 from Gram-positive bacteria encodes a resolvase, designated Res beta, which shares homology with the proteins of the resolvase-invertase family [4].
• The resolvase/invertase domain of the site-specific recombinase TnpX is functional and recognizes a target sequence that resembles the junction of the circular form of the Clostridium perfringens transposon Tn4451 [5].

High impact information on rsvA

• Architecture of the gamma delta resolvase synaptosome: oriented heterodimers identity interactions essential for synapsis and recombination [6].
• The 2,3' interaction between resolvase dimers is essential for synapsis and recombination [6].
• In vitro recombination by Tn3 resolvase of plasmids containing two directly repeated recombination (res) sites generates two singly interlinked catenated rings [7].
• A putative binding site may be located in the N-terminal portion of the TnpR (resolvase) structural gene sequences [8].
• Examination of the Tn501 DNA sequence also reveals a potential tnpM coding sequence upstream of the Tn501 resolvase gene [8].

Chemical compound and disease context of rsvA

• Evidence that phenylalanine 69 in Escherichia coli RuvC resolvase forms a stacking interaction during binding and destabilization of a Holliday junction DNA substrate [9].
• Norfloxacin-induced DNA cleavage occurs at the dif resolvase locus in Escherichia coli and is the result of interaction with topoisomerase IV [10].

Biological context of rsvA

• Immediately upstream of the bfp gene cluster, we identified a potential replication origin including genes that are predicted to encode proteins homologous with replicase and resolvase [11].
• Substrate specificity of RusA resolvase reveals the DNA structures targeted by RuvAB and RecG in vivo [12].
• To dissect the pathways of Holliday junction processing in a eukaryote, we have targeted an Escherichia coli Holliday junction resolvase to the nuclei of fission yeast recombination-deficient mutants and analysed their phenotypes [3].
• Our results demonstrate the functional autonomy of the resolvase catalytic domain and open the way to creating "custom-built" recombinases that act at chosen natural target sequences [13].
• The dif resolvase locus of the Escherichia coli chromosome can be replaced by a 33-bp sequence, but function depends on location [14].

Associations of rsvA with chemical compounds

• The intermediate accumulates at low reaction temperatures and is stabilized by crosslinking of the resolvase protomers with glutaraldehyde [15].
• Induction of the transcriptional fusions results in production of resolvase, which in turn, catalyzes excision of a linked tetracycline-resistance reporter gene flanked by direct repeats of res, the DNA sequences at which resolvase functions [16].
• With one exception, where a glutamate residue had been replaced by leucine, the activity of these mutants was similar to that of wild-type Tn21 resolvase [17].
• We propose a model for Tn4451 excision and insertion in which the resolvase/invertase domain of TnpX introduces 2-bp staggered cuts at these GA dinucleotides [5].
• Tn1739tnpR is a derivative of Tn1721 with a chloramphenicol-resistance-encoding gene (CmR), the lambda cI repressor gene, and a further copy of the resolvase-encoding tnpR gene under control of the tac promoter [18].

Analytical, diagnostic and therapeutic context of rsvA

• We have isolated in quantitative yield the synaptic intermediate formed during site-specific recombination by Tn3 resolvase and characterized it by restriction endonuclease mapping, electron microscopy and topological methods [15].
• We used site-directed mutagenesis to investigate such residues in the RusA resolvase [19].
• We have constructed a genetic bioassay for inhibitors of site-specific recombination by transposon Tn3 resolvase [20].

References