Laboratory of Biophysical Chemistry of Macromolecules, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
J Mol Biol. 2021 Mar 19;433(6):166676. doi: 10.1016/j.jmb.2020.10.010. Epub 2020 Oct 14.
The centromere is an essential chromatin domain required for kinetochore recruitment and chromosome segregation in eukaryotes. To perform this role, centro-chromatin adopts a unique structure that provides access to kinetochore proteins and maintains stability under tension during mitosis. This is achieved by the presence of nucleosomes containing the H3 variant CENP-A, which also acts as the epigenetic mark defining the centromere. In this review, we discuss the role of CENP-A on the structure and dynamics of centromeric chromatin. We further discuss the impact of the CENP-A binding proteins CENP-C, CENP-N, and CENP-B on modulating centro-chromatin structure. Based on these findings we provide an overview of the higher order structure of the centromere.
着丝粒是真核生物中用于动粒募集和染色体分离的必需染色质结构域。为了发挥这一作用，着丝粒染色质采用了一种独特的结构，为动粒蛋白提供了进入的途径，并在有丝分裂过程中保持张力下的稳定性。这是通过含有 H3 变体 CENP-A 的核小体的存在来实现的，CENP-A 也作为定义着丝粒的表观遗传标记。在这篇综述中，我们讨论了 CENP-A 在着丝粒染色质结构和动力学中的作用。我们进一步讨论了 CENP-A 结合蛋白 CENP-C、CENP-N 和 CENP-B 对调节中心染色质结构的影响。基于这些发现，我们提供了着丝粒高级结构的概述。
