TY - JOUR
T1 - Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex
AU - Seo, Sang beom
AU - Macfarlan, Todd
AU - McNamara, Peter
AU - Hong, Rui
AU - Mukai, Yuki
AU - Heo, Soyoung
AU - Chakravarti, Debabrata
PY - 2002/4/19
Y1 - 2002/4/19
N2 - Histone acetylation by p300/CBP and PCAF coactivators is considered to be a key mechanism of chromatin modification and transcriptional regulation. A multiprotein cellular complex, INHAT (inhibitor of acetyltransferases), containing the Set/TAF-Iβ oncoprotein and pp32 strongly inhibits the HAT activity of p300/CBP and PCAF by histone masking. Here we report that the INHAT complex and its subunits have overlapping but distinct HAT inhibitory and histone binding characteristics. We provide evidence suggesting that the histone binding and INHAT activity of pp32 can be regulated by its physical association with other INHAT subunits. In vivo colocalization and transfection studies show that pp32 INHAT domains are responsible for histone binding, HAT inhibitory activity, and repression of transcription. We propose that INHAT and its subunits may function by modulating histone acetyltransferases through a histone-masking mechanism and may play important regulatory roles in the establishment and maintenance of the newly proposed "histone code" of chromatin.
AB - Histone acetylation by p300/CBP and PCAF coactivators is considered to be a key mechanism of chromatin modification and transcriptional regulation. A multiprotein cellular complex, INHAT (inhibitor of acetyltransferases), containing the Set/TAF-Iβ oncoprotein and pp32 strongly inhibits the HAT activity of p300/CBP and PCAF by histone masking. Here we report that the INHAT complex and its subunits have overlapping but distinct HAT inhibitory and histone binding characteristics. We provide evidence suggesting that the histone binding and INHAT activity of pp32 can be regulated by its physical association with other INHAT subunits. In vivo colocalization and transfection studies show that pp32 INHAT domains are responsible for histone binding, HAT inhibitory activity, and repression of transcription. We propose that INHAT and its subunits may function by modulating histone acetyltransferases through a histone-masking mechanism and may play important regulatory roles in the establishment and maintenance of the newly proposed "histone code" of chromatin.
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U2 - 10.1074/jbc.M112455200
DO - 10.1074/jbc.M112455200
M3 - Article
C2 - 11830591
AN - SCOPUS:0037134538
SN - 0021-9258
VL - 277
SP - 14005
EP - 14010
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 16
ER -