5ikf
From Proteopedia
Crystal structure of the C-terminal domain of the Mit1 nucleosome remodeler in complex with Clr1
Structural highlights
FunctionMIT1_SCHPO Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).[1] Publication Abstract from PubMedNucleosome remodeling and deacetylation (NuRD) complexes are co-transcriptional regulators implicated in differentiation, development, and diseases. Methyl-CpG binding domain (MBD) proteins play an essential role in recruitment of NuRD complexes to their target sites in chromatin. The related SHREC complex in fission yeast drives transcriptional gene silencing in heterochromatin through cooperation with HP1 proteins. How remodeler and histone deacetylase (HDAC) cooperate within NuRD complexes remains unresolved. We determined that in SHREC the two modules occupy distant sites on the scaffold protein Clr1 and that repressive activity of SHREC can be modulated by the expression level of the HDAC-associated Clr1 domain alone. Moreover, the crystal structure of Clr2 reveals an MBD-like domain mediating recruitment of the HDAC module to heterochromatin. Thus, SHREC bi-functionality is organized in two separate modules with separate recruitment mechanisms, which work together to elicit transcriptional silencing at heterochromatic loci. SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules.,Job G, Brugger C, Xu T, Lowe BR, Pfister Y, Qu C, Shanker S, Banos Sanz JI, Partridge JF, Schalch T Mol Cell. 2016 Apr 21;62(2):207-21. doi: 10.1016/j.molcel.2016.03.016. PMID:27105116[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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