5IKF

Crystal structure of the C-terminal domain of the Mit1 nucleosome remodeler in complex with Clr1

Summary for 5IKF

• Entry DOI: 10.2210/pdb5ikf/pdb
• Descriptor: Chromatin remodeling factor mit1, Cryptic loci regulator protein 1, ZINC ION, ... (5 entities in total)
• Functional Keywords: zinc fingers, alpha-helical, protein-protein interface, complex, transcription
• Biological source: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); More
• Cellular location: Nucleus: Q9P793 O74808
• Total number of polymer chains: 2
• Total formula weight: 47214.95

Authors

Brugger, C.,Schalch, T. (deposition date: 2016-03-03, release date: 2016-04-20, Last modification date: 2024-05-08)

Primary citation

Job, G.,Brugger, C.,Xu, T.,Lowe, B.R.,Pfister, Y.,Qu, C.,Shanker, S.,Banos Sanz, J.I.,Partridge, J.F.,Schalch, T.
SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules.
Mol.Cell, 62:207-221, 2016

PubMed Abstract: Nucleosome 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.

PubMed: 27105116
DOI: 10.1016/j.molcel.2016.03.016

Experimental method

X-RAY DIFFRACTION (2.8 Å)