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Toward a consensus on the binding specificity and promiscuity of PRC2 for RNA.

Mol. Cell. 2015 Feb 05;57(3):552-8. Epub 2015 Jan 15
Chen Davidovich 1 , Xueyin Wang 1 , Catherine Cifuentes-Rojas 2 , Karen J Goodrich 1 , Anne R Gooding 1 , Jeannie T Lee 3 , Thomas R Cech 4
Chen Davidovich 1 , Xueyin Wang 1 , Catherine Cifuentes-Rojas 2 , Karen J Goodrich 1 , Anne R Gooding 1 , Jeannie T Lee 3 , Thomas R Cech 4
+ et al

[No authors listed]

Author information
  • 1 Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, BioFrontiers Institute, University of Colorado, Boulder, CO 80309, USA.
  • 2 Howard Hughes Medical Institute, Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
  • 3 Howard Hughes Medical Institute, Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA. Electronic address: lee@molbio.mgh.harvard.edu.
  • 4 Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, BioFrontiers Institute, University of Colorado, Boulder, CO 80309, USA. Electronic address: thomas.cech@colorado.edu.

摘要

Polycomb repressive complex-2 (PRC2) is a histone methyltransferase required for epigenetic silencing during development and cancer. Early works suggested binding specificity of PRC2 to certain long non-coding RNAs for recruitment to chromatin. More recent studies provided evidence both in favor and against this idea. Here, we bridge the two existing models of PRC2-RNA interaction. RepA RNA is a good binding partner for PRC2, while multiple non-relevant RNAs, including bacterial mRNAs, also bind PRC2; Kds depend to some extent on the experimental conditions. Human and mouse PRC2 have broadly similar RNA-binding properties in vitro. Examination of evidence supporting an existing model for site-specific recruitment of PRC2 by a well-defined RNA motif in cells reveals that results are PRC2 independent. We conclude that promiscuous and specific RNA-binding activities of PRC2 in vitro are not mutually exclusive, and that binding specificity in vivo remains to be demonstrated.

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