Molecular characterization of Celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2

Staal, Ada; Enserink, Jorrit M.; Stein, Janet L.; Wijnen, André J. van

doi:10.1002/1097-4652(200011)185:2<269::aid-jcp12>3.0.co;2-l

Cited by 36 publications

(20 citation statements)

References 52 publications

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“…We have shown that, in addition to BRCA1, BRD7 is also able to recruit the transcription factor Oct-1 to the ESR1 promoter. A previous study showed that BRD7 could also bind the transcription factor IRF2 (13). It is possible that the role of BRD7 within the Swi/ Snf complex is to provide specificity by selectively recruiting specific transcription factors.…”

Section: Discussionmentioning

confidence: 99%

BRD7, a Subunit of SWI/SNF Complexes, Binds Directly to BRCA1 and Regulates BRCA1-Dependent Transcription

et al. 2010

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We carried out a yeast two-hybrid screen using a BRCA1 bait composed of amino acids 1 to 1142 and identified BRD7 as a novel binding partner of BRCA1. This interaction was confirmed by coimmunoprecipitation of endogenous BRCA1 and BRD7 in T47D and HEK-293 cells. BRD7 is a bromodomain containing protein, which is a subunit of PBAF-specific Swi/Snf chromatin remodeling complexes. To determine the functional consequences of the BRCA1-BRD7 interaction, we investigated the role of BRD7 in BRCA1-dependent transcription using microarray-based expression profiling. We found that a variety of targets were coordinately regulated by BRCA1 and BRD7, such as estrogen receptor α (ERα). Depletion of BRD7 or BRCA1 in either T47D or MCF7 cells resulted in loss of expression of ERα at both the mRNA and protein level, and this loss of ERα was reflected in resistance to the antiestrogen drug fulvestrant. We show that BRD7 is present, along with BRCA1 and Oct-1, on the ESR1 promoter (the gene which encodes ERα). Depletion of BRD7 prevented the recruitment of BRCA1 and Oct-1 to the ESR1 promoter; however, it had no effect on the recruitment of the other Swi/Snf subunits BRG1, BAF155, and BAF57 or on RNA polymerase II recruitment. These results support a model whereby the regulation of ERα transcription by BRD7 is mediated by its recruitment of BRCA1 and Oct-1 to the ESR1 promoter. Cancer Res; 70(6); 2538-47. ©2010 AACR.

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Section: Discussionmentioning

confidence: 99%

BRD7, a Subunit of SWI/SNF Complexes, Binds Directly to BRCA1 and Regulates BRCA1-Dependent Transcription

et al. 2010

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“…Kzhyshkowska et al (2003) suggested that BRD7, together with E1B-AP5, which belongs to the family of hnRNP-u, functioned as an inhibitor of basic transcription in several viral and cellular promoters in the nucleus. Staal et al (2000) reported that the BRD7 protein (celtix-1) interacted with interferon regulatory factor 2 (IRF-2) in the nucleus and was associated with transcriptionally active chromatin in situ. In addition, Kim et al (2003) reported that BP75, the most homologous gene of BRD7, was found to bind dishevelled-1 and enhance Wnt signaling by inactivating glycogen synthase kinase-3 beta.…”

Section: Introductionmentioning

confidence: 99%

Cloning and Characterization of the BRD7 Gene Promoter

Liu¹,

Peng²,

Zhou³

et al. 2006

DNA and Cell Biology

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BRD7, a novel bromodomain gene, encodes a protein that inhibits cell growth and cell cycle progression by transcriptional regulation of some cell cycle-related genes. Its transcriptional down-expression has been shown to be critical to the pathogenesis of Nasopharyngeal carcinoma (NPC). Little is known about the transcriptional mechanisms controlling BRD7 gene expression. In this paper, we have characterized the 5' regulatory region of the BRD7 gene in order to understand the molecular mechanisms regulating its expression. Transient transfection results suggested that the analyzed upstream sequences of the BRD7 gene might contain some important but not sufficient sequence information to confer the cell-type specificity of BRD7 gene expression. Further analysis with a series of deletions demonstrated that a 125-bp region was required for the basal promoter activity of the BRD7 gene. Results from ChIP and EMSA indicated that the promoter was responsive to Sp1, E2F, and E2F6. All of these suggest a possible mechanism that transcriptional factor Sp1, E2F, and E2F-6 are associated in the BRD7 promoter region and regulate BRD7 promoter activity. Taken together, these results will help to better understand the role of the BRD7 gene in signal-dependent transcriptional regulation, and to develop new reagents for therapeutic upregulation of the BRD7 gene in NPC.

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“…The variation in the ΔC p values between specific and nonspecific BrD3-acetyl-histone complexes determined experimentally was compared with the values calculated based on the change in solvent-exposed surface area [47][48][49]: (5) where ΔA np and ΔA p are the changes in nonpolar and polar surface area, respectively. The ΔC p values from nonspecific to specific range from -400 to -1600 J/K · mol, indicating significant variation in the hydration of the BrD-histone interface.…”

Section: Discussionmentioning

confidence: 99%

“…Mounting evidence indicates that large multiprotein chromatin remodeling complexes regulate transcription by localizing to certain chromatin sites through the interaction of bromodomain (BrD) 1 proteins with acetylated nucleosomes [1][2][3][4][5][6][7]. The BrD is a protein motif, approximately 100 amino acids in length, primarily associated with targeting subunits of chromatin remodeling complexes [8].…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic analysis of acetylation-dependent Pb1 bromodomain–histone H3 interactions

Thompson

Chandrasekaran

2008

Analytical Biochemistry

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An acetyl-histone peptide library was used to determine the thermodynamic parameters that define acetylation-dependent bromodomain-histone interactions. Bromodomains interact with histones by binding acetylated lysines. The bromodomain used in this study, BrD3, is derived from the polybromo-1 protein, which is a subunit of the PBAF chromatin remodeling complex. Steady-state fluorescence anisotropy was used to examine the variations in specificity and affinity that drive molecular recognition. Temperature and salt concentration dependence studies demonstrate that the hydrophobic effect is the primary driving force, consistent with lysine acetylation being required for binding. An electrostatic effect was observed in only two complexes where the acetyl-lysine was adjacent to an arginine. The large change in heat capacity determined for the specific complex suggests that the dehydrated BrD3-histone interface forms a tightly bound, high-affinity complex with the target site. These explorations into the thermodynamic driving forces that confer acetylation site-dependent BrD3-histone interactions improve our understanding of how individual bromodomains work in isolation. Furthermore, this work will permit the development of hypotheses regarding how the native Pb1, and the broader class of bromodomain proteins, directs multisubunit chromatin remodeling complexes to specific acetyl-nucleosome sites in vivo. KeywordsAcetyl-lysine; Histone acetylation; Polybromo; Histone code; Protein-protein interactions; Thermodynamics Histone acetylation is a key regulator of transcription; however, it is still a matter of debate as to whether the regulatory features are influenced by modification at specific lysine sites or it is the cumulative electrostatic consequences of random lysine acetylation. Mounting evidence indicates that large multiprotein chromatin remodeling complexes regulate transcription by localizing to certain chromatin sites through the interaction of bromodomain (BrD) 1 proteins with acetylated nucleosomes [1][2][3][4][5][6][7]. The BrD is a protein motif, approximately 100 amino acids in length, primarily associated with targeting subunits of chromatin remodeling complexes [8]. The biological role of the BrD centers on its ability to discriminate the acetylation state of lysine residues in histone proteins. In fact, there is growing evidence that the position of the acetyl-lysine is not random, but instead, the BrD requires acetylation at specific sites for highaffinity binding [9]. For example, fluorescence resonance energy transfer assays were used to show that the bromodomain protein Brd2 requires the interaction between its bromodomain and an acetyl-histone to amplify transcription in vivo [10]. To activate transcription after SAGA (Spt-Ada-Gcn5 acetyl-transferase) complex directed acetylation at specific nucleosomal locations, BrD proteins of the Swi2/Snf2 complex are required to displace acetyl-histones [11]. Likewise, the yeast RSC (remodels the structure of chromatin) complex requires multiple BrD...

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Molecular characterization of Celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2

Cited by 36 publications

References 52 publications

BRD7, a Subunit of SWI/SNF Complexes, Binds Directly to BRCA1 and Regulates BRCA1-Dependent Transcription

BRD7, a Subunit of SWI/SNF Complexes, Binds Directly to BRCA1 and Regulates BRCA1-Dependent Transcription

Cloning and Characterization of the BRD7 Gene Promoter

Thermodynamic analysis of acetylation-dependent Pb1 bromodomain–histone H3 interactions

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