L3MBTL2 protein acts in concert with PcG protein-mediated monoubiquitination of H2A to establish a repressive chromatin structure.

@article{Trojer2011L3MBTL2PA,
  title={L3MBTL2 protein acts in concert with PcG protein-mediated monoubiquitination of H2A to establish a repressive chromatin structure.},
  author={Patrick Trojer and Alina R. Cao and Zhonghua Gao and Yan Li and Jin Zhang and Xiaoqin Xu and Guohong Li and R{\'e}gine Losson and Hediye Erdjument-Bromage and Paul Tempst and Peggy J. Farnham and Danny F Reinberg},
  journal={Molecular cell},
  year={2011},
  volume={42 4},
  pages={438-50}
}
We have identified human MBT domain-containing protein L3MBTL2 as an integral component of a protein complex that we termed Polycomb repressive complex 1 (PRC1)-like 4 (PRC1L4), given the copresence of PcG proteins RING1, RING2, and PCGF6/MBLR. PRC1L4 also contained E2F6 and CBX3/HP1γ, known to function in transcriptional repression. PRC1L4-mediated repression necessitated L3MBTL2 that compacted chromatin in a histone modification-independent manner. Genome-wide location analyses identified… CONTINUE READING
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