H3K27 methylation and H3S28 phosphorylation-dependent transcriptional regulation by INHAT subunit SET/TAF-Iβ

Ji Young Kim; Kee Beom Kim; Hye Ju Son; Yun Cheol Chae; Si Taek Oh; Dong Wook Kim; Jhang Ho Pak; Sang Beom Seo

doi:10.1016/j.febslet.2012.06.026

H3K27 methylation and H3S28 phosphorylation-dependent transcriptional regulation by INHAT subunit SET/TAF-Iβ

Ji Young Kim, Kee Beom Kim, Hye Ju Son, Yun Cheol Chae, Si Taek Oh, Dong Wook Kim, Jhang Ho Pak, Sang Beom Seo

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me1/2/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene.

Original language	English
Pages (from-to)	3159-3165
Number of pages	7
Journal	FEBS Letters
Volume	586
Issue number	19
DOIs	https://doi.org/10.1016/j.febslet.2012.06.026
State	Published - 21 Sep 2012

Keywords

H3K27me
H3S28 Phosphorylation
INHAT
Peptide array
SET/TAF-Iβ

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10.1016/j.febslet.2012.06.026

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title = "H3K27 methylation and H3S28 phosphorylation-dependent transcriptional regulation by INHAT subunit SET/TAF-Iβ",

abstract = "Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me1/2/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene.",

keywords = "H3K27me, H3S28 Phosphorylation, INHAT, Peptide array, SET/TAF-Iβ",

author = "Kim, {Ji Young} and Kim, {Kee Beom} and Son, {Hye Ju} and Chae, {Yun Cheol} and Oh, {Si Taek} and Kim, {Dong Wook} and Pak, {Jhang Ho} and Seo, {Sang Beom}",

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doi = "10.1016/j.febslet.2012.06.026",

language = "English",

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T1 - H3K27 methylation and H3S28 phosphorylation-dependent transcriptional regulation by INHAT subunit SET/TAF-Iβ

AU - Kim, Ji Young

AU - Kim, Kee Beom

AU - Son, Hye Ju

AU - Chae, Yun Cheol

AU - Oh, Si Taek

AU - Kim, Dong Wook

AU - Pak, Jhang Ho

AU - Seo, Sang Beom

PY - 2012/9/21

Y1 - 2012/9/21

N2 - Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me1/2/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene.

AB - Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me1/2/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene.

KW - H3K27me

KW - H3S28 Phosphorylation

KW - INHAT

KW - Peptide array

KW - SET/TAF-Iβ

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DO - 10.1016/j.febslet.2012.06.026

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SN - 0014-5793

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SP - 3159

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JO - FEBS Letters

JF - FEBS Letters

IS - 19

ER -

H3K27 methylation and H3S28 phosphorylation-dependent transcriptional regulation by INHAT subunit SET/TAF-Iβ

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Keywords

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