The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism
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DOI: 10.1038/s41467-019-08314-x
Abstract: Centromeric nucleosomes are composed of the centromere-specific histone H3 variant CENP-A and the core histones H2A, H2B, and H4. To establish a functional kinetochore, histone H4 lysine-20 (H4K20) must be monomethylated, but the underlying mechanism… read more here.
Keywords: targeting domain; cenp; cenp centromere; centromere targeting ... See more keywords
Structural basis of nucleosomal histone H4 lysine 20 methylation by SET8 methyltransferase
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DOI: 10.26508/lsa.202000919
Abstract: Cryo-EM structures of the human SET8–nucleosome complexes reveal the mechanism by which the SET8 methyltransferase binds the nucleosome and specifically recognizes the histone H4 lysine-20 residue. SET8 is solely responsible for histone H4 lysine-20 (H4K20)… read more here.
Keywords: set8; h4k20 monomethylation; histone lysine; set8 methyltransferase ... See more keywords