6VHF

Crystal structure of RbBP5 interacting domain of Cfp1

Summary for 6VHF

• Entry DOI: 10.2210/pdb6vhf/pdb
• Descriptor: PHD-type domain-containing protein, ZINC ION (3 entities in total)
• Functional Keywords: histone, mll, cfp1, rbbp5, compass, epigenetics, peptide binding protein
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• Total number of polymer chains: 1
• Total formula weight: 24836.15

Authors

Joshi, M.,Couture, J.F. (deposition date: 2020-01-09, release date: 2020-01-22, Last modification date: 2024-04-03)

Primary citation

Yang, Y.,Joshi, M.,Takahashi, Y.H.,Ning, Z.,Qu, Q.,Brunzelle, J.S.,Skiniotis, G.,Figeys, D.,Shilatifard, A.,Couture, J.F.
A non-canonical monovalent zinc finger stabilizes the integration of Cfp1 into the H3K4 methyltransferase complex COMPASS.
Nucleic Acids Res., 48:421-431, 2020

PubMed Abstract: COMPlex ASsociating with SET1 (COMPASS) is a histone H3 Lys-4 methyltransferase that typically marks the promoter region of actively transcribed genes. COMPASS is a multi-subunit complex in which the catalytic unit, SET1, is required for H3K4 methylation. An important subunit known to regulate SET1 methyltransferase activity is the CxxC zinc finger protein 1 (Cfp1). Cfp1 binds to COMPASS and is critical to maintain high level of H3K4me3 in cells but the mechanisms underlying its stimulatory activity is poorly understood. In this study, we show that Cfp1 only modestly activates COMPASS methyltransferase activity in vitro. Binding of Cfp1 to COMPASS is in part mediated by a new type of monovalent zinc finger (ZnF). This ZnF interacts with the COMPASS's subunits RbBP5 and disruption of this interaction blunts its methyltransferase activity in cells and in vivo. Collectively, our studies reveal that a novel form of ZnF on Cfp1 enables its integration into COMPASS and contributes to epigenetic signaling.

PubMed: 31724694
DOI: 10.1093/nar/gkz1037

Experimental method

X-RAY DIFFRACTION (2.311 Å)