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. 2016 Sep;26(9):1178–1187. doi: 10.1101/gr.204784.116

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© 2016 Thakur and Henikoff; Published by Cold Spring Harbor Laboratory Press

This article, published in Genome Research, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 7. — A model for the CENPA/CENPB/CENPC/CENPT chromatin complex. (Left) Hypothesized arrangement of CENPA, B, C, and T along a single 340-bp Cen1-like dimeric unit. (Middle) During interphase, the CENPT complex occupies the CENPB box-containing linker on young 340-bp α-satellite dimers between tandem CENPA nucleosomes. Each CENPA particle binds a CENPC on one side and wraps ∼100-bp DNA with right-handed chirality. (Right) At anaphase, tension causes the positively supercoiled DNA to overwind and tighten up around the complex, favoring stacking of tandem dimers to form a stiff platform that spreads pulling forces.