5OQD

PHD2 and winged-helix domain of Polycomblike

Summary for 5OQD

• Entry DOI: 10.2210/pdb5oqd/pdb
• Descriptor: Polycomb protein Pcl, ZINC ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: polycomblike, winged-helix domain, phd finger domain, gene regulation
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Nucleus : Q24459
• Total number of polymer chains: 6
• Total formula weight: 153923.36

Authors

Choi, J.,Benda, C.,Mueller, J. (deposition date: 2017-08-11, release date: 2017-11-01, Last modification date: 2024-05-08)

Primary citation

Choi, J.,Bachmann, A.L.,Tauscher, K.,Benda, C.,Fierz, B.,Muller, J.
DNA binding by PHF1 prolongs PRC2 residence time on chromatin and thereby promotes H3K27 methylation.
Nat. Struct. Mol. Biol., 24:1039-1047, 2017

PubMed Abstract: Polycomb repressive complex 2 (PRC2) trimethylates histone H3 at lysine 27 to mark genes for repression. We measured the dynamics of PRC2 binding on recombinant chromatin and free DNA at the single-molecule level using total internal reflection fluorescence (TIRF) microscopy. PRC2 preferentially binds free DNA with multisecond residence time and midnanomolar affinity. PHF1, a PRC2 accessory protein of the Polycomblike family, extends PRC2 residence time on DNA and chromatin. Crystallographic and functional studies reveal that Polycomblike proteins contain a winged-helix domain that binds DNA in a sequence-nonspecific fashion. DNA binding by this winged-helix domain accounts for the prolonged residence time of PHF1-PRC2 on chromatin and makes it a more efficient H3K27 methyltranferase than PRC2 alone. Together, these studies establish that interactions with DNA provide the predominant binding affinity of PRC2 for chromatin. Moreover, they reveal the molecular basis for how Polycomblike proteins stabilize PRC2 on chromatin and stimulate its activity.

PubMed: 29058710
DOI: 10.1038/nsmb.3488

Experimental method

X-RAY DIFFRACTION (2.447 Å)