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Histone octamer function in vivo: mutations in the dimer-tetramer interfaces disrupt both gene activation and repression.
Within the core histone octamer each histone H4 interacts with each H2A-H2B dimer subunit through two binding surfaces. Tyrosines play a central role in these interactions with H4 tyrosines 72 and 88 contacting one H2A-H2B dimer subunit, and tyrosine 98 contacting the other. To investigate the roles...
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| Autores principales: | , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
1997
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1169849/ https://ncbi.nlm.nih.gov/pubmed/9171362 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/16.9.2493 |
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