ArticleBiophysical journal2014
CENP-A arrays are more condensed than canonical arrays at low ionic strength.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Nanoscale analysis of human G1 and metaphase chromatin in situ.The EMBO journal · 2025Article
- Combining per-particle cryo-ET and cryo-EM single particle analysis to elucidate heterogeneous DNA-protein organization.Current opinion in structural biology · 2024Review
- CENP-A and CENP-B collaborate to create an open centromeric chromatin state.Nature communications · 2023Article
- CENP-A nucleosome-a chromatin-embedded pedestal for the centromere: lessons learned from structural biology.Essays in biochemistry · 2020Review
- Natural chromatin is heterogeneous and self-associates in vitro.Molecular biology of the cell · 2018Article
- CENP-A and topoisomerase-II antagonistically affect chromosome length.The Journal of cell biology · 2017Article
- Epigenetic origin of evolutionary novel centromeres.Scientific reports · 2017Article
- Internal modifications in the CENP-A nucleosome modulate centromeric dynamics.Epigenetics & chromatin · 2017Article
- The molecular basis for centromere identity and function.Nature reviews. Molecular cell biology · 2016Review
- A cell-free CENP-A assembly system defines the chromatin requirements for centromere maintenance.The Journal of cell biology · 2015Article
- Structural transitions of centromeric chromatin regulate the cell cycle-dependent recruitment of CENP-N.Genes & development · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The centromeric histone H3 variant centromeric protein A (CENP-A), whose sequence is the least conserved among all histone variants, is responsible for specifying the location of the centromere. Here, we present a comprehensive study of CENP-A nucleosome arrays by cryo-electron tomography. We see that CENP-A arrays have different biophysical properties than canonical ones under low ionic conditions, as they are more condensed with a 20% smaller average nearest-neighbor distance and a 30% higher nucleosome density. We find that CENP-A nucleosomes have a predominantly crossed DNA entry/exit site that is narrowed on average by 8°, and they have a propensity to stack face to face. We therefore propose that CENP-A induces geometric constraints at the nucleosome DNA entry/exit site to bring neighboring nucleosomes into close proximity. This specific property of CENP-A may be responsible for generating a fundamental process that contributes to increased chromatin fiber compaction that is propagated under physiological conditions to form centromeric chromatin.
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Registered trials
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