In vivo complex formation of PU.1 with HDAC1 associated with PU.1-mediated transcriptional repression

Kihara-Negishi, Fumiko; Yamamoto, Hiroaki; Suzuki, Motoo; Yamada, Toshiyuki; Sakurai, Takeshi; Tamura, Tomohiro; Oikawa, Tsuneyuki

doi:10.1038/sj.onc.1204756

Cited by 59 publications

(59 citation statements)

References 48 publications

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“…MeCP2 DRC mutant may be able to recruit mSin3A to the N-terminal region of MeCP2 as reported by an other group (Nan et al, 1998). Alternatively, this mutant may recruit mSin3A-HDAC through binding to PU.1, since PU.1 interacts directly with the mSin3A-HDAC1 complex through the regions surrounding the Ets domain as we previously reported (Kihara-Negishi et al, 2001). This interaction might be implicated in the repression of PU.1 activity in this setting.…”

Section: Discussionmentioning

confidence: 73%

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Direct association between PU.1 and MeCP2 that recruits mSin3A-HDAC complex for PU.1-mediated transcriptional repression

et al. 2003

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Section: Discussionmentioning

confidence: 73%

“…As mentioned above, we showed the direct interaction of PU.1 with mSin3A (Kihara-Negishi et al, 2001). On the other hand, we also previously demonstrated the direct interaction of PU.1 with transcriptional coactivator CBP, which enhances transcriptional activity of PU.1 (Yamamoto et al, 1999).…”

Section: Discussionmentioning

confidence: 76%

Direct association between PU.1 and MeCP2 that recruits mSin3A-HDAC complex for PU.1-mediated transcriptional repression

et al. 2003

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“…We have previously reported that PU.1 interacts with CRE-binding protein (CBP) or p300, which functions as a coactivator for several transcription factors . We have also demonstrated that PU.1 binds to the corepressor mSin3A and forms a complex with histone deacetyl transferase (HDAC)1 (Kihara-Negishi et al, 2001). Moreover, we have reported that MeCP2 is a binding partner of the PU.1-mSin3A-HDAC complex, but not of the PU.1-CBP complex (Suzuki et al, 2003).…”

Section: Introductionmentioning

confidence: 98%

Site-specific DNA methylation by a complex of PU.1 and Dnmt3a/b

et al. 2005

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The Ets transcription factor PU.1 is a hematopoietic master regulator essential for the development of myeloid and B-cell lineages. As we previously reported, PU.1 sometimes represses transcription on forming a complex with mSin3A-histone deacetyl transferase-MeCP2. Here, we show an interaction between PU.1 and DNA methyltransferases, DNA methyltransferase (Dnmt)3a and Dnmt3b (Dnmt3s). Glutathione-S-transferase pulldown assay revealed that PU.1 directly interacted with the ATRX domain of Dnmt3s through the ETS domain. Dnmt3s repressed the transcriptional activity of PU.1 on a reporter construct with trimerized PU.1-binding sites. The repression was recovered by addition of 5-aza-deoxycitidine, a DNA methyltransferase inhibitor, but not trichostatin A, a histone deacetylase inhibitor. Bisulfite sequence analysis revealed that several CpG sites in the promoter region neighboring the PU.1-binding sites were methylated when Dnmt3s were coexpressed with PU.1. We also showed that the CpG sites in the p16 INK4A promoter were methylated by overexpression of PU.1 in NIH3T3 cells, accompanied by a downregulation of p16 INK4A gene expression. These results suggest that PU.1 may downregulate its target genes through an epigenetic modification such as DNA methylation.

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“…Y Nakazawa et al previously that PU.1, another member of the ETS family, also forms a complex with mSin3A/HDAC1 and MeCP2 under certain conditions (Kihara-Negishi et al, 2001;Suzuki et al, 2003;Hwang et al, 2004). Therefore, ETS1 might also be able to recruit transcriptional corepressors.…”

Section: Ets1-gfi1 Interaction In the Repression Of Bax Gene Expressionmentioning

confidence: 99%

Cooperative interaction between ETS1 and GFI1 transcription factors in the repression of Bax gene expression

et al. 2007

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The proto-oncoproteins ETS1 and growth factor independent-1 (GFI1) are implicated in cell growth and differentiation in various types of cells, and their deregulated expression is involved in malignant transformation. Here, we report that ETS1 and GFI1 interact and affect gene expression through their cross-talk. Co-immunoprecipitation analyses and glutathione-S-transferase pull-down assays revealed that ETS1 bound directly to GFI1 via its Ets domain, and GFI1 bound to ETS1 via its zincfinger domain. Luciferase (Luc) assays using artificial reporters showed that GFI1 repressed ETS1-mediated transcriptional activation and ETS1 repressed GFI1-mediated transcriptional activation, in a dose-dependent manner. However, in the Bax promoter where the Ets-and Gfi-binding sites (EBS and GBS) are adjacent, ETS1 and GFI1 cooperatively reduced activation. Site-directed mutagenesis on the EBS and GBS of the Bax promoter showed that both binding sites were necessary for full repression. Chromatin immunoprecipitation analyses confirmed that an ETS1-GFI1 complex formed on the Bax promoter even when either EBS or GBS was mutated. Introduction of small interfering RNA against ETS1 and/ or GFI1 enhanced endogenous Bax gene expression. Our results suggest that the interaction between ETS1 and GFI1 facilitates their binding to specific sites on the Bax promoter and represses Bax expression in vivo.

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In vivo complex formation of PU.1 with HDAC1 associated with PU.1-mediated transcriptional repression

Cited by 59 publications

References 48 publications

Direct association between PU.1 and MeCP2 that recruits mSin3A-HDAC complex for PU.1-mediated transcriptional repression

Direct association between PU.1 and MeCP2 that recruits mSin3A-HDAC complex for PU.1-mediated transcriptional repression

Site-specific DNA methylation by a complex of PU.1 and Dnmt3a/b

Cooperative interaction between ETS1 and GFI1 transcription factors in the repression of Bax gene expression

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