The Elusive Structure of Centro-Chromatin: Molecular Order or Dynamic Heterogenetity?
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.
['Nagpal|Harsh|H|', 'Fierz|Beat|B|']
D000251:Adenosine Triphosphatases D018797:Cell Cycle Proteins D002503:Centromere D000076247:Centromere Protein A D051936:Centromere Protein B D002843:Chromatin D002868:Chromosomal Proteins, Non-Histone D004268:DNA-Binding Proteins D044127:Epigenesis, Genetic D006801:Humans D008938:Mitosis D008958:Models, Molecular D046912:Multiprotein Complexes D009690:Nucleic Acid Conformation D011485:Protein Binding D000072756:Protein Conformation, alpha-Helical D000072757:Protein Conformation, beta-Strand D054730:Protein Interaction Domains and Motifs D012441:Saccharomyces cerevisiae
centromere chromatin kinetochore CENP-A