Text Size:AAA

Histone Modifying Enzyme

Histone modifying enzymes catalyze the addition or removal of an array of covalent modifications in histone and non-histone proteins. Within the context of chromatin, these modifications regulate gene expression as well as other genomic functions and have been implicated in establishing and maintaining a heritable epigenetic code that contributes to defining cell identity and fate. Biochemical and structural characterization of histone modifying enzymes has yielded important insights into their respective catalytic mechanisms, substrate specificities, and regulation.

Sino Biological offers a comprehensive set of tools for Histone-modifying related studies, including recombinant proteins, antibodies (rabbit mAbs, mouse mAbs, rabbit pAbs), ELISA kits, and ORF cDNA clones.

Product CategoriesProteinsAntibodiesELISA KitscDNA Clones
Number of Products

Histone Modifying Enzyme Related Products Index

    Histone Modifying Enzyme Related Products by Product Type

    Histone Modifying Enzyme Background

    Histone modifying enzymes catalyze the addition or removal of an array of covalent modifications in histone and non-histone proteins. Within the context of chromatin, these modifications regulate gene expression as well as other genomic functions and have been implicated in establishing and maintaining a heritable epigenetic code that contributes to defining cell identity and fate. Biochemical and structural characterization of histone modifying enzymes has yielded important insights into their respective catalytic mechanisms, substrate specificities, and regulation.

    Two classes of enzymes reversibly control the acetylation level of histones: histone acetyltransferases (HATs) and histone deacetylases (HDACs). In general, transcriptional activators recruit HATs, whereas transcriptional repressors and co-repressors associate with HDACs. Translocation, amplification, overexpression, or mutation of HAT genes occurs in a variety of cancers, especially those of hematological and epithelial origin. HDACs facilitate chromatin folding and also affect the binding of regulatory factors to nucleosomal targets. These enzymes are classified into three different groups (I, II, III) on the basis of their sequence homology to the yeast HDACs.

    Histone methylation is more complex than acetylation. Both lysines and arginines can be methylated. Lysines can be mono-, di-, or tri-methylated. Arginines can be either mono- or di-methylated, and arginine dimethylation may be asymmetric or symmetric. The positions of many methylated residues in histones H3 and H4 have been mapped. The complexities in the types and levels of methylation provide much regulatory potential as each event may have specific effects on chromatin structure and on the interactions of regulatory proteins with chromatin.

    Several histones and histone variants are subject to phosphorylation, including H1, H3, H2B, and H2A. These modifications are associated with large scale chromatin reorganization during processes such as mitosis, apoptosis, and DNA repair. As aberrant execution of these processes facilitates cancer formation, improper regulation, or function of the kinases that mediate histone phosphorylation can be oncogenic.

    Many histone modifying enzymes also use non-histone proteins as substrates. The activities of HATs, HDACs, and histone arginine methyltransferases on non-histone substrates are well documented, but only a few examples of lysine methylation within non-histone substrates have yet been reported.

    Histone Modifying Enzyme References

      1. Marmorstein R, et al. (2009) Histone modifying enzymes: structures, mechanisms, and specificities. Biochim Biophys Acta. 1789(1): 58-68.
      2. Zhang K, et al. (2005) Histone modifying enzymes and cancer: going beyond histones. J Cell Biochem. 96(6): 1137-48.
      3. Gibbons RJ. (2005) Histone modifying and chromatin remodelling enzymes in cancer and dysplastic syndromes. Hum Mol Genet. 14(1): 85-92.