Histones are the main protein component of chromatin and are essential for the storage and compaction of the genome. DNA wraps around histone oligomers to make up nucleosomes, the individual subunits of chromatin. By altering the accessibility of the genome, chromatin structure is important for regulating various cellular processes including replication, transcription, and DNA repair. Typically chromatin structure is influenced by post-translational modification of histone proteins at lysine and arginine residues. These residues are concentrated at the amino-terminal end of the histone protein and can alter its interaction with the DNA or recruit and bind to chromatin remodeling complexes. The complex language of histone modifications creates multiple levels of gene regulation and also forms the basis for epigenetic regulation. Of the core histones, H2A, H2B, H3, and H4 can all be modified by methylation, phosphorylation, acetylation, or ubiquitination. Modifications of H3, also known as H3.1, have been well studied and are linked to the regulation of various aspects of gene expression. For example, trimethylation of lysine 4 (H3K4me3) is typically found at transcription start sites and correlates with actively transcribed genes. Trimethylation of lysine 9 (H3K9me3), on the other hand, is associated with transcriptional repression. Investigating the interactome of histones and their modifications is an essential step to developing a comprehensive understanding of global gene regulation (1). Modern research techniques such as RNA-Seq and ChIP-Seq in conjunction with tools such as H3.1 antibodies targeting specific histone modifications have allowed great strides towards these goals.
Genome-wide analysis of histone modifications using ChIP-Seq provides insight into global gene regulation and also serves as an excellent resource for researchers to examine the chromatin context at their gene of interest. One of these genome-wide histone maps from the Gutierrez lab at UCLA used H3.1 antibodies to examine the distribution of histone modifications across the Arabidopsis genome (2). Examination of histone distribution during development also provides information about histone modifications during gene regulation. A recent study by Harada et al. used H3.1 antibodies specific for various histone modifications in their examination of myogenic differentiation (3). By altering the ratio of H3.1 to H3.3 variant, the authors were able to characterize histone modifications during skeletal muscle differentiation (3). The epigenetic functions of histone modification, especially during meiosis, remains an area with high interest. Research using H3.1 antibodies examined the histone dynamics of condensation and decondensation of the genome during Drosophila spermatogenesis (4). This study identified histone modifications unique to the male germ line and also identified variable modification patterns between autosomal and sex chromosomes (4). The ability of H3.1 antibodies to differentiate highly similar yet distinct histone modifications has allowed researchers to perform detailed analysis of diverse biological processes. The variety of tools and techniques available to visualize or quantify histone modifications has continued to grow and has greatly increased our understanding of genome regulation.
Novus Biologicals offers Histone H3.1 reagents for your research needs including:
Histone H3.1 antibodies
Histone H3.1 lysates
Histone H3.1 proteins
Histone H3.1 RNAi
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