Structural highlights
Function
ADDA_BACSU An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' -> 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.[1] [2] [3]
References
- ↑ Kooistra J, Haijema BJ, Venema G. The Bacillus subtilis addAB genes are fully functional in Escherichia coli. Mol Microbiol. 1993 Mar;7(6):915-23. PMID:8387145
- ↑ Chedin F, Ehrlich SD, Kowalczykowski SC. The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro. J Mol Biol. 2000 Apr 21;298(1):7-20. PMID:10756102 doi:http://dx.doi.org/10.1006/jmbi.2000.3556
- ↑ Yeeles JT, Dillingham MS. A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases. J Mol Biol. 2007 Aug 3;371(1):66-78. Epub 2007 May 25. PMID:17570399 doi:http://dx.doi.org/10.1016/j.jmb.2007.05.053
