Title : Contact site of histones 2A and 2B in chromatin and in solution.

Pub. Date : 1985 May 21

PMID : 4027221






2 Functional Relationships(s)
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1 Sequence analysis of the peptides isolated from the H2A-H2B dimer formed in solution and in nuclei demonstrated that both dimers are produced through the covalent linkage of Tyr-40 of H2B and Pro-26 of H2A. Proline H2B clustered histone 21 Homo sapiens
2 We conclude that the precise juxtaposition of Tyr-40 of H2B and Pro-26 of H2A in this region of the H2A/H2B contact site is not altered upon interaction of these histones with H3 and H4 (tetramer), DNA, or other chromosomal components during nucleosome assembly. Proline H2B clustered histone 21 Homo sapiens