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Deficient histone acetylation in acute leukemia and the correction by an isothiocyanate

Liyun Xiao1, Yiqun Huang, Ruiji Zhen

  • 1Department of Hematology, Zhangzhou Affiliated Hospital of Fujian Medical University, Zhangzhou, China.

Acta Haematologica
|January 7, 2010
PubMed
Abstract

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Histone Modification02:32

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...