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Results 1 - 10 of 11 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5malfunction individual null-mutations of all three genes, recC, recB, and recD, or the deletion of whole recCBD operon of Pseudomonas syringae, lead to growth inhibition at low temperature, and sensitivity to UV and mitomycin C. Viability of the mutant cells drops drastically at 4°C, and the mutants accumulate linear chromosomal DNA and shorter DNA fragments in higher amounts compared to 22°C -, 716691
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5metabolism enzyme RecBCD's repair of DNA is controlled by Chi, overview 751756
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5metabolism the RecBCD/AddAB complexes are highly processive helicase/nuclease machines that digest DNA from the broken end until they encounter a crossover hotspot instigator (Chi) sequence. At this point their activities are modulated to produce a 3-tailed duplex onto which RecA is loaded 750403
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5more the SH3 domain interacts with the ssDNA tail in a location different to that normally occupied by a peptide in canonical eukaryotic SH3 domains, thus retaining the potential to bind peptide at the same time as the ssDNA tail, interactions with the 5'-tail and the RecD subunit, overview. The N-terminal domain of RecD contacts the 2B domain of RecC and the conformational change in RecD has significant effects on the conformation of the RecC subunit. The RecB nuclease domain bridges a gap between the 1A and 2B domains of RecC and the conformational changes cause a significant shift in position of the RecB nuclease relative to these domains that reveals the mechanism for nuclease activation. Interaction between the 2B domain of RecD and the RecB subunit has a number of consequences, analysis of conformational changes that proceed from the initiation complex to nuclease activation 750403
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5more the tether (amino acids 881-899) of RecB is essential for Chi's stimulation of recombination. The tether can be lengthened somewhat without alteration of Chi's control, but a too-long tether significantly reduces Chi's control of RecBCD 751756
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5physiological function after transposition of phage Mu into the Escherichia coli chromosome, the flanking DNA is degraded, and the 5-bp gaps left in the target are repaired to generate a simple Mu insertion. The first event in repair is removal of the flanking DNA by RecBCD exonuclease, whose entry past the N-protein block is licensed by the transpososome. When RecBCD is allowed entry into the flanking DNA, it degrades this DNA until it arrives at the transpososome, which presents a barrier for further RecBCD movement. RecBCD action is required for stimulating endonucleolytic cleavage within the transpososome-protected DNA, leaving 4-nt flanks outside both Mu ends 730828
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5physiological function RecBCD (exonuclease V) plays a critical role in recombinational DNA repair. Escherichia coli RecBCD is involved in recombinational repair of double-strand breaks that are caused by defective DNA replication and other DNA damaging agents. Unrepaired DNA damage caused by cisplatin or UV light can lead to defective DNA replication and the production of double-strand breaks. Presence of adducts on the DNA double-helix can have major consequences for the efficient functioning of DNA repair enzymes. Escherichia coli RecBCD (exonuclease V) is involved in recombinational repair of double-strand breaks that are caused by defective DNA replication, DNA damaging agents and other factors. The holoenzyme possesses a bipolar helicase activity which helps unwind DNA from both 3'- and 5'-directions and is coupled with a potent exonuclease activity that is also capable of digesting DNA from both 3'- and 5'-ends 749820
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5physiological function RecBCD-type helicase-nuclease (RecBCD) catalyses the processing of double-stranded DNA breaks for repair by homologous recombination. The enzyme complex is a highly processive, duplex unwinding and degrading machine that requires tight regulation. The nuclease activity of the complex is activated once unwinding progresses 750403
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5physiological function RecD associates with two other proteins RecB and RecC to produce RecBCD enzyme, which is involved in homologous recombination and DNA repair in many bacteria, including Escherichia coli. All three subunits of the RecBCDPs enzyme are essential for DNA repair and growth of Pseudomonas syringae at low temperatures of 4°C. The RecD requirement is only a function of the RecBCD complex in the bacterium. The RecBCD pathway protects the Antarctic bacterium from cold-induced DNA damages, and is critically dependent on the helicase activities of both RecB and RecD subunits, but not on the nuclease of RecBCDPs enzyme -, 716691
Display the word mapDisplay the reaction diagram Show all sequences 3.1.11.5physiological function repair of DNA double-strand breaks uses a highly conserved helicase-nuclease complex to unwind DNA from a broken end and cut it at specific DNA sequences called Chi. In Escherichia coli the RecBCD enzyme also loads the DNA strand exchange protein RecA onto the newly formed end, resulting in a recombination hotspot at Chi. Chi hotspots regulate multiple RecBCD activities by altering RecBCD's conformation, which is proposed to include the swinging of the RecB nuclease domain on the 19-amino-acid tether connecting the helicase and nuclease domains. Proper control of RecBCD by Chi requires that the tether be long enough and appropriately flexible. A model, in which the swing-time of the nuclease domain determines the position of Chi-dependent and Chi-independent cuts and Chi hotspot activity, is established. Generation of a molecular model for Chi-dependent nuclease swinging, and predictions of the nuclease-swing model, overview 751756
Results 1 - 10 of 11 > >>