||RuvAB catalyzes strand migration by an ATP-dependent mechanism [PUB_0532]. RuvA tetramers unfold the junction in a square planar conformation [PUB_0532]. RuvB hexamers possess DNA-dependent ATPase activity that is stimulated by RuvA [PUB_0536]. Although there is 1 ATP binding site per RuvB monomer, each hexamer only binds 2 ATPs, only 1 of which is hydrolyzed [PUB_0537]. Junction migration occurs in discrete hops of mean length 2.2 bases [PUB_0538] at a rate 3-100 bp/s [PUB_0531, PUB_0532, PUB_0533, PUB_0534, PUB_0535, PUB_0538]. Junctions are preferentially resolved at the sequence 5'-(A/T)TT↓(G/C)-3' [PUB_0532].
Dawid A, Croquette V, Grigoriev M, Heslot F. Single-molecule study of RuvAB-mediated Holliday-junction migration. Proc Natl Acad Sci U S A 101, 11611-6 (2004). WholeCell: PUB_0532, PubMed: 15292508
Dennis C, Fedorov A, Käs E, Salomé L, Grigoriev M. RuvAB-directed branch migration of individual Holliday junctions is impeded by sequence heterology. EMBO J 23, 2413-22 (2004). WholeCell: PUB_0534, PubMed: 15167893
Grigoriev M, Hsieh P. Migration of a Holliday junction through a nucleosome directed by the E. coli RuvAB motor protein. Mol Cell 2, 373-81 (1998). WholeCell: PUB_0535, PubMed: 9774975
Karymov MA, Chinnaraj M, Bogdanov A, Srinivasan AR, Zheng G, Olson WK, Lyubchenko YL. Structure, dynamics, and branch migration of a DNA Holliday junction: a single-molecule fluorescence and modeling study. Biophys J 95, 4372-83 (2008). WholeCell: PUB_0538, PubMed: 18658216
Kowalczykowski SC, Dixon DA, Eggleston AK, Lauder SD, Rehrauer WM. Biochemistry of homologous recombination in Escherichia coli. Microbiol Rev 58, 401-65 (1994). WholeCell: PUB_0536, PubMed: 7968921
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