| First Author | Southall SM | Year | 2014 |
| Journal | Nucleic Acids Res | Volume | 42 |
| Issue | 1 | Pages | 661-71 |
| PubMed ID | 24049080 | Mgi Jnum | J:211428 |
| Mgi Id | MGI:5575440 | Doi | 10.1093/nar/gkt776 |
| Citation | Southall SM, et al. (2014) A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases. Nucleic Acids Res 42(1):661-71 |
| abstractText | The delivery of site-specific post-translational modifications to histones generates an epigenetic regulatory network that directs fundamental DNA-mediated processes and governs key stages in development. Methylation of histone H4 lysine-20 has been implicated in DNA repair, transcriptional silencing, genomic stability and regulation of replication. We present the structure of the histone H4K20 methyltransferase Suv4-20h2 in complex with its histone H4 peptide substrate and S-adenosyl methionine cofactor. Analysis of the structure reveals that the Suv4-20h2 active site diverges from the canonical SET domain configuration and generates a high degree of both substrate and product specificity. Together with supporting biochemical data comparing Suv4-20h1 and Suv4-20h2, we demonstrate that the Suv4-20 family enzymes take a previously mono-methylated H4K20 substrate and generate an exclusively di-methylated product. We therefore predict that other enzymes are responsible for the tri-methylation of histone H4K20 that marks silenced heterochromatin. |
