2RPH
RecT-bound ssDNA
Summary for 2RPH
Entry DOI | 10.2210/pdb2rph/pdb |
Related | 2RPD 2RPE 2RPF |
NMR Information | BMRB: 11048 |
Descriptor | DNA (5'-D(*DTP*DAP*DCP*DG)-3') (1 entity in total) |
Functional Keywords | ssdna, rect, reca, dna |
Total number of polymer chains | 1 |
Total formula weight | 1190.83 |
Authors | Masuda, T.,Ito, Y.,Shibata, T.,Mikawa, T. (deposition date: 2008-05-15, release date: 2009-05-26, Last modification date: 2024-05-15) |
Primary citation | Masuda, T.,Ito, Y.,Terada, T.,Shibata, T.,Mikawa, T. A non-canonical DNA structure enables homologous recombination in various genetic systems J.Biol.Chem., 284:30230-30239, 2009 Cited by PubMed Abstract: Homologous recombination, which is critical to genetic diversity, depends on homologous pairing (HP). HP is the switch from parental to recombinant base pairs, which requires expansion of inter-base pair spaces. This expansion unavoidably causes untwisting of the parental double-stranded DNA. RecA/Rad51-catalyzed ATP-dependent HP is extensively stimulated in vitro by negative supercoils, which compensates for untwisting. However, in vivo, double-stranded DNA is relaxed by bound proteins and thus is an unfavorable substrate for RecA/Rad51. In contrast, Mhr1, an ATP-independent HP protein required for yeast mitochondrial homologous recombination, catalyzes HP without the net untwisting of double-stranded DNA. Therefore, we questioned whether Mhr1 uses a novel strategy to promote HP. Here, we found that, like RecA, Mhr1 induced the extension of bound single-stranded DNA. In addition, this structure was induced by all evolutionarily and structurally distinct HP proteins so far tested, including bacterial RecO, viral RecT, and human Rad51. Thus, HP includes the common non-canonical DNA structure and uses a common core mechanism, independent of the species of HP proteins. We discuss the significance of multiple types of HP proteins. PubMed: 19729448DOI: 10.1074/jbc.M109.043810 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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