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Vol. 16, No. 22, pp. 2893-2905, November 15, 2002
1 Howard Hughes Medical Institute, Division of Nucleic
Acids Enzymology, Department of Biochemistry, University of
Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical
School, Piscataway, New Jersey 08854, USA; 2 Molecular Biology
Program, Memorial Sloan Kettering Cancer Center, New York,
New York 10021, USA
Enhancer of Zeste [E(z)] is a Polycomb-group transcriptional
repressor and one of the founding members of the family of SET domain-containing proteins. Several SET-domain proteins possess intrinsic histone methyltransferase (HMT) activity. However,
recombinant E(z) protein was found to be inactive in a HMT assay. Here
we report the isolation of a multiprotein E(z) complex that contains extra sex combs, suppressor of zeste-12 [Su(z)12], and the histone binding proteins RbAp46/RbAp48. This complex, which we termed Polycomb
repressive complex (PRC) 2, possesses HMT activity with specificity for
Lys 9 (K9) and Lys 27 (K27) of histone H3. The HMT activity of PRC2 is
dependent on an intact SET domain in the E(z) protein. We hypothesize
that transcriptional repression by the E(z) protein involves
methylation-dependent recruitment of PRC1. The presence of Su(z)12, a
strong suppressor of position effect variegation, in PRC2 suggests that
PRC2 may play a widespread role in heterochromatin-mediated silencing.
[Key Words: Histone methylation; Polycomb; SET domain; transcription repression; chromatin]
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