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• W2495057506 abstract "Histone proteins are essential for the organization, expression, and inheritance of genetic material for eukaryotic cells. A centromere-specific H3 histone variant, centromere protein A (CENP-A), shares about 50% amino acid sequence identity with H3. CENP-A is required for packaging the centromere and for the proper separation of chromosomes during mitosis. Despite their distinct biological functions, previously reported crystal structures of the CENP-A/H4 and H3/H4 dimers reveal a high degree of similarity. In this work, we characterize the structural dynamics of CENP-A/H4 and H3/H4 dimers based on a dual-resolution approach, using both microsecond-scale explicit-solvent all-atom and coarse-grained (CG) molecular dynamics (MD) simulations. Our data show that the H4 histone is significantly more rigid compared with the H3 histone and its variant CENP-A, hence, serving as a reinforcing structural element within the histone core. We report that the CENP-A/H4 dimer is significantly more dynamic than its cano..." @default.
• W2495057506 created "2016-08-23" @default.
• W2495057506 creator A5005357908 @default.
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• W2495057506 date "2016-08-12" @default.
• W2495057506 modified "2023-09-23" @default.
• W2495057506 title "Promiscuous Histone Mis-Assembly Is Actively Prevented by Chaperones" @default.
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• W2495057506 doi "https://doi.org/10.1021/jacs.6b05355" @default.
• W2495057506 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7757119" @default.
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• W2495057506 hasPublicationYear "2016" @default.
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