Transcriptional activation by GAGA factor is through its direct interaction with dmTAF3

Chopra, Vivek S.; Srinivasan, Arumugam; Kumar, Ram P.; Mishra, Krishnaveni; Basquin, Denis; Docquier, Mylène; Seum, Carole; Pauli, Daniel; Mishra, Rakesh

doi:10.1016/j.ydbio.2008.02.008

Cited by 47 publications

(45 citation statements)

References 62 publications

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“…GAGA factor might open up the chromatin structure by interacting with the chromatin remodeling factor nucleosome remodeling factor (NURF; Xiao et al 2001) and the histone chaperon, Facilitates Chromatin Transcription (FACT) (Nakayama et al 2007). GAGA factor has also recently been found to interact with a subunit of TFIID, thus allowing GAGA factor to facilitate preinitiation complex formation (Chopra et al 2008).…”

Section: Positioned Nucleosomes Might Contribute To Promoter Proximalmentioning

confidence: 99%

Promoter proximal pausing on genes in metazoans

Gilmour

2008

Chromosoma

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The past two decades of research into transcriptional control of protein-encoding genes in eukaryotes have focused on regulatory mechanisms that act by controlling the recruitment of Pol II to a gene's promoter. Recent genome-wide analyses of the distribution of Pol II indicates that Pol II is concentrated in the promoter regions of thousands of genes in human and Drosophila cells. In many cases, Pol II may have initiated transcription but paused in the promoter proximal region. Hence, release of Pol II from the promoter region into the body of a gene is now recognized as a common rate-limiting step in the control of gene expression. Notably, most genes with paused Pol II are expressed indicating that the pause can be transient. What causes Pol II to concentrate in the promoter region and how it is released to transcribe a gene are the focus of this review.

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Section: Positioned Nucleosomes Might Contribute To Promoter Proximalmentioning

confidence: 99%

Promoter proximal pausing on genes in metazoans

Gilmour

2008

Chromosoma

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“…10 A significant amount of data indicates that BTB domains are involved in the recruitment of non-BTB-containing regulator proteins. [11][12][13] Another set of experiments have shown that BTB domains of different proteins in some cases can specifically interact with each other, but it is unknown how such interactions proceed. Rarely, heterodimerization of two different BTBs has been observed.…”

Section: Introductionmentioning

confidence: 99%

Drosophila BTB/POZ Domains of “ttk Group” Can Form Multimers and Selectively Interact with Each Other

Bonchuk

Denisov

Georgiev

et al. 2011

Journal of Molecular Biology

103

109

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Edited by M. GottesmanKeywords: GAGA; BTB domain; Mod(mdg4); CP190; chromatin insulatorThe BTB (bric-a-brac, tramtrack and broad complex)/POZ (poxvirus and zinc finger) domain is a conserved protein-protein interaction motif contained in a variety of transcription factors involved in development, chromatin remodeling, insulator activity, and carcinogenesis. All wellstudied mammalian BTB domains form obligate homodimers and, rarely, tetramers. Only the BTB domain of the Drosophila GAGA factor (GAF) has been shown to exist as higher-order multimers. The BTB domain of GAF belongs to the "ttk group" that contains several highly conserved sequences not found in other BTB domains. Here, we have shown by size-exclusion chromatography, chemical cross-linking, and nondenaturing PAGE that four additional BTB domains of the ttk group-Batman, Mod(mdg4), Pipsqueak, and Tramtrack-can form multimers, like GAF. Interestingly, the BTB domains of GAF and Batman have formed a wide range of complexes and interacted in the yeast two-hybrid assay with other BTB domains tested. In contrast, the BTB domains of Mod(mdg4), Pipsqueak, and Tramtrack have formed stable high-order multimer complexes and failed to interact with each other. The BTB domain of Drosophila CP190 protein does not belong to the ttk group. This BTB domain has formed stable dimers and has not interacted with domains of the ttk group. Previously, it was suggested that GAF oligomerization into higher-order complexes facilitates long-range activation by providing a protein bridge between an enhancer and a promoter. Unexpectedly, experiments in the Drosophila model system have not supported the role of GAF in organization of longdistance interaction between the yeast GAL4 activator and the white promoter.© 2011 Elsevier Ltd. All rights reserved. IntroductionThe BTB (bric-a-brac, tramtrack and broad complex) domain [also known as the POZ (poxvirus and zinc finger) domain] is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcription regulation (for review, see Ref. 1 ). Transcription factors with a BTB domain at the N-terminus comprise a large important class of molecules involved in development and carcinogenesis. As shown in crystallographic studies,

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“…A few BTB-zinc finger proteins, including Drosophila GAGA factor, also have the ability to activate transcription (Biggin and Tjian 1988;Staller et al 2001;Rodova et al 2004). Recently, the GAGA factor BTB domain was shown to bind to the TAFIID general transcription factor subunit TAF-3, suggesting that the GAGA factor may function as a transcriptional activator by recruiting the core TAFIID machinery to its target promoters (Chopra et al 2008). In general, 1 however, much less is known about protein interactions of the BTB domain in BTB-zinc finger proteins that function as activators.…”

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confidence: 99%

EOR-2 Is an Obligate Binding Partner of the BTB–Zinc Finger Protein EOR-1 in Caenorhabditis elegans

et al. 2010

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BTB-zinc finger transcription factors play many important roles in metazoan development. In these proteins, the BTB domain is critical for dimerization and for recruiting cofactors to target genes. Identification of these cofactors is important for understanding how BTB-zinc finger proteins influence transcription. Here we show that the novel but conserved protein EOR-2 is an obligate binding partner of the BTB-zinc finger protein EOR-1 in Caenorhabditis elegans. EOR-1 and EOR-2 function together to promote multiple Ras/ERK-dependent cell fates during development, and we show that EOR-1 is a robust substrate of ERK in vitro. A point mutation (L81F) in the EOR-1 BTB domain reduces both ERK phosphorylation and EOR-2 binding and eliminates all detectable biological function without affecting EOR-1 expression levels, localization, or dimerization. This point mutation lies near the predicted charged pocket region of the EOR-1 BTB dimer, a region that, in other BTB-zinc finger proteins, has been proposed to interact with corepressors or coactivators. We also show that a conserved zinc finger-like motif in EOR-2 is required for binding to EOR-1, that the interaction between EOR-1 and EOR-2 is direct, and that EOR-2 can bind to the human BTB-zinc finger protein PLZF. We propose that EOR-2 defines a new family of cofactors for BTB-zinc finger transcription factors that may have conserved roles in other organisms.

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Transcriptional activation by GAGA factor is through its direct interaction with dmTAF3

Cited by 47 publications

References 62 publications

Promoter proximal pausing on genes in metazoans

Promoter proximal pausing on genes in metazoans

Drosophila BTB/POZ Domains of “ttk Group” Can Form Multimers and Selectively Interact with Each Other

EOR-2 Is an Obligate Binding Partner of the BTB–Zinc Finger Protein EOR-1 in Caenorhabditis elegans

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