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Vol. 16, No. 8, pp. 919-932, April 15, 2002
The Wistar Institute, Philadelphia, Pennsylvania 19104, USA
Posttranslational modification of histones has emerged as a key
regulatory signal in eukaryotic gene expression. Recent genetic and
biochemical studies link H3-lysine 9 (H3-K9) methylation to HP1-mediated heterochromatin formation and gene silencing. However, the
mechanisms that target and coordinate these activities to specific
genes is poorly understood. Here we report that the KAP-1 corepressor
for the KRAB-ZFP superfamily of transcriptional silencers binds to
SETDB1, a novel SET domain protein with histone H3-K9-specific methyltransferase activity. Although acetylation and phosphorylation of
the H3 N-terminal tail profoundly affect the efficiency of H3-K9
methylation by SETDB1, we found that methylation of H3-K4 does not
affect SETDB1-mediated methylation of H3-K9. In vitro methylation of
the N-terminal tail of histone H3 by SETDB1 is sufficient to enhance
the binding of HP1 proteins, which requires both an intact chromodomain
and chromoshadow domain. Indirect immunofluoresence staining of
interphase nuclei localized SETDB1 predominantly in euchromatic regions
that overlap with HP1 staining in nonpericentromeric regions of
chromatin. Moreover, KAP-1, SETDB1, H3-MeK9, and HP1 are enriched at
promoter sequences of a euchromatic gene silenced by the
KRAB-KAP-1 repression system. Thus, KAP-1 is a molecular
scaffold that is targeted by KRAB-ZFPs to specific loci and coordinates
both histone methylation and the deposition of HP1 proteins to silence
gene expression.
[Key Words: Histone methylation; SET domain; chromatin; KRAB domain]
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