Histone methylation and ubiquitination with their cross-talk and roles in gene expression and stability.
Methylation of lysine residues of histones is associated with functionally distinct regions of chromatin, and, therefore, is an important epigenetic mark. Over the past few years, several enzymes that catalyze this covalent modification on different lysine residues of histones have been discovered. Intriguingly, histone lysine methylation has also been shown to be cross-regulated by histone ubiquitination or the enzymes that catalyze this modification. These covalent modifications and their cross-talks play important roles in regulation of gene expression, heterochromatin formation, genome stability, and cancer. Thus, there has been a very rapid progress within past several years towards elucidating the molecular basis of histone lysine methylation and ubiquitination, and their aberrations in human diseases. Here, we discuss these covalent modifications with their cross-regulation and roles in controlling gene expression and stability.
Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, 62901, USA.
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Shukla
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Chaurasia
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Bhaumik
D004260:DNA Repair; D005786:Gene Expression Regulation; D006657:Histones / Q000378:metabolism* / Q000502:physiology*; D008745:Methylation; D055550:Protein Stability; D020239:Receptor Cross-Talk; D054875:Ubiquitination
D006657:Histones