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Histone acetyltransferase HBO1 inhibits NF-kappaB activity by coactivator sequestration.

Abstract：

:The MYST acetyltransferase HBO1 is implicated in the regulation of DNA replication and activities of transcription factors such as the androgen receptor. Since the androgen receptor and NF-kappaB transcription factors crossmodulate their transcriptional activity, we investigated whether HBO1 regulates NF-kappaB signaling. Here, we report that in 293T cells HBO1 reduced dose-dependently NF-kappaB activity stimulated by TNFalpha, or by overexpressing p65/RelA, RelB, or cRel. Mutational analysis showed that the N-terminal serine-rich region of HBO1 but not the acetyltransferase function was required for inhibition. Electrophoretic mobility-shift assays demonstrated that HBO1 was neither perturbing the formation of p65/RelA DNA complexes nor binding itself to the kappaB consensus sequence or to p65/RelA, suggesting that HBO1 reduced NF-kappaB activity by squelching a cofactor. These data establish a novel function for HBO1 showing that it reduced NF-kappaB activity by sequestrating an essential coactivator from the NF-kappaB transcriptional complex.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Contzler R,Regamey A,Favre B,Roger T,Hohl D,Huber M

doi

10.1016/j.bbrc.2006.09.030

subject

Has Abstract

pub_date

2006-11-10 00:00:00

pages

208-13

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)02054-7

journal_volume

350

pub_type

杂志文章

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