2001
DOI: 10.1006/dbio.2001.0358
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The BTB/POZ Domain of the Regulatory Proteins Bric à brac 1 (BAB1) and Bric à brac 2 (BAB2) Interacts with the Novel Drosophila TAFII Factor BIP2/dTAFII155

Abstract: The BTB/POZ domain is an evolutionarily conserved protein-protein interaction domain present in the N-terminal region of numerous transcription factors involved in development, chromatin remodeling, and human cancers. This domain is involved in homomeric and heteromeric associations with other BTB/POZ domains. The Drosophila BTB/POZ proteins Bric à brac 1 (BAB1) and Bric à brac 2 (BAB2) are developmentally regulated transcription factors which are involved in pattern formation along the proximo-distal axis of … Show more

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Cited by 35 publications
(32 citation statements)
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“…TAFs have been known to act as specific coactivators by interacting with transcriptional activators, and TAFs contribute to promoter recognition and selectivity (Verrijzer et al, 1994;Burke and Kadonaga, 1997). BIP2 was first identified as a partner of the Bric à brac 2 (Bab2) protein (Pointud et al, 2001). BAB2 interacts with BIP2 via BTB/POZ domains, and these two proteins colocalize at transcriptionally active regions of polytene chromosomes (Pointud et al, 2001).…”
Section: Expression Of Vas and Nos Rna In Pole Cells Of The Dsrna-injmentioning
confidence: 99%
“…TAFs have been known to act as specific coactivators by interacting with transcriptional activators, and TAFs contribute to promoter recognition and selectivity (Verrijzer et al, 1994;Burke and Kadonaga, 1997). BIP2 was first identified as a partner of the Bric à brac 2 (Bab2) protein (Pointud et al, 2001). BAB2 interacts with BIP2 via BTB/POZ domains, and these two proteins colocalize at transcriptionally active regions of polytene chromosomes (Pointud et al, 2001).…”
Section: Expression Of Vas and Nos Rna In Pole Cells Of The Dsrna-injmentioning
confidence: 99%
“…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%
“…Bab2 was also shown to bind at discrete sites along polytene chromosomes (D. Godt, unpubl. data;Pointud et al, 2001), suggesting that Bab1 and Bab2 function as transcriptional regulators.…”
mentioning
confidence: 99%
“…Both genes encode proteins with a BTB domain and a pipsqueak motif (Couderc et al, 2002), domains found in a number of transcriptional regulators (Collins, 2001;Lehmann, 1998). Both Bab1 and Bab2 are localized to the nucleus (Couderc et al, 2002;Godt and Laski, 1995;Godt et al, 1993) and interact with BIP2/ TAF II 155, a component of TFIID (Pointud et al, 2001). Bab2 was also shown to bind at discrete sites along polytene chromosomes (D. Godt, unpubl.…”
mentioning
confidence: 99%