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<p></p> <p><b>新页面</b></p><div>Condensin. (A) Condensin is a five-subunit protein complex that resembles cohesin <br /> (see Figure 17–23). The ATPase head domains of its two major subunits, Smc2 and Smc4, are <br /> held together by a linker protein called Brn1, which is associated with two additional proteins called <br /> Ycs4 and Ycg1. (B) These diagrams illustrate a mechanism by which condensin might generate <br /> DNA loops, thereby promoting the compaction of a chromosome. For an alternative model, see <br /> Figure 4–56. In the model shown here, the process begins when the Ycg1 subunit interacts tightly <br /> with a strand of chromosome DNA, anchoring the condensin firmly in place on the DNA. The <br /> nearby DNA curls around to interact with the hinge domain. By mechanisms that remain unclear, <br /> the hinge and ATPase domains work together, using energy from ATP hydrolysis, to move leftward <br /> along the top DNA strand (red arrow), thereby generating a chromosome loop. Such loops are <br /> common structural elements in chromosome packaging (discussed in Chapter 4).</div>

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