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Biology LibreTexts

8.11: Branch Migration

The movement of a Holliday junction to generate additional heteroduplex requires two proteins. One is the RuvA tetramer, which recognizes the structure of the Holliday junction. A rendering of the structure derived from X-ray crystallographic analysis of the RuvA-Holliday junction crystals is shown in Fig. 8.18.

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Figure 8.18: Three-dimensional structure of the RuvA tetramer complexed with a Holliday junction [from Hargreaves et al. (1998) Nature Structural Biology 5: 441-4460]. For the RuvA protein, alpha helices are green cylinders, beta sheets are brown arrows and loops are blue. The four strands of the two duplexes in the Holliday junction are red lines. The atomic coordinates were downloaded from the Molecular Structure database at NCBI, rendered in Cn3D v.3.0, and a pict file obtained as a screen shot. The kin file for viewing the virtual 3-D image on your own computer is accessible at the course web site.

RuvB is an ATPase. It forms hexameric rings that provide the motor for branch migration. As illustrated in Fig. 8.19, RuvA tetramers recognize the Holliday junction, and RuvB uses the energy of ATP hydrolysis to unwind the parental duplexes and form heteroduplexes between them.

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Figure 8.19: Branch migration of RuvA-RuvB in solution. The four monomers of RuvA combine around a central pen to accommodate the square planar configuration of the Holliday junction in which the four DNA duplex arms attach to grooves on the concave surface of RuvA. Through ATP hydrolysis, the two hexameric RuvB rings encircle and translocate the dsDNA arms. Curved arrows indicate rotation of DNA while the thick arrows indicate translocation of dsDNA through the junction. DNA rotation during Holliday junction branch occurs at a V(max) of 1.6 revolutions per second, or 8.3 bp per second. Adopted from reference Eggleston, A. K. and West, S. C. (1996) Trends in Genetics 12: 20-25. Image used with permission (Public Domain).