| First Author | Maison C | Year | 2016 |
| Journal | Nat Commun | Volume | 7 |
| Pages | 12224 | PubMed ID | 27426629 |
| Mgi Jnum | J:240822 | Mgi Id | MGI:5896477 |
| Doi | 10.1038/ncomms12224 | Citation | Maison C, et al. (2016) The methyltransferase Suv39h1 links the SUMO pathway to HP1alpha marking at pericentric heterochromatin. Nat Commun 7:12224 |
| abstractText | The trimethylation of histone H3 on lysine 9 (H3K9me3) - a mark recognized by HP1 that depends on the Suv39h lysine methyltransferases (KMTs) - has provided a basis for the reader/writer model to explain HP1 accumulation at pericentric heterochromatin in mammals. Here, we identify the Suv39h1 paralog, as a unique enhancer of HP1alpha sumoylation both in vitro and in vivo. The region responsible for promoting HP1alpha sumoylation (aa1-167) is distinct from the KMT catalytic domain and mediates binding to Ubc9. Tethering the 1-167 domain of Suv39h1 to pericentric heterochromatin, but not mutants unable to bind Ubc9, accelerates the de novo targeting of HP1alpha to these domains. Our results establish an unexpected feature of Suv39h1, distinct from the KMT activity, with a major role for heterochromatin formation. We discuss how linking Suv39h1 to the SUMO pathway provides conceptual implications for our general view on nuclear domain organization and physiological functions. |
