Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors.

Nakajima, Takeshi; Uchida, Chiharu; Anderson, Stephen F.; Parvin, Jeffrey D.; Montminy, Marc

doi:10.1101/gad.11.6.738

Cited by 227 publications

(217 citation statements)

References 28 publications

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“…(b) Western blot analysis of nuclear extract from A431 cells using anti-BRCA1 antibody after immunoprecipitation with anti-BRCA1 antibody was done as described (Cui et al, 1998b). The protein bands shown represent endogenous BRCA1a (p110) and BRCA1b (p100) proteins BRCA1 associates with RNA polymerase II holoenzyme complex (Scully et al, 1997a) and CBP (CREBbinding protein) is a component of the holoenzyme (Nakajima et al, 1997). Previously, we have found BRCA1a/p110 and BRCA1b/p100 to interact both in vitro and in vivo with the carboxy-terminal domain of transcription factor CBP (Cui et al, 1998b).…”

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confidence: 99%

The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter

et al. 1999

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Inherited mutations in the breast and ovarian cancer susceptibility gene BRCA1 are associated with high risk for developing breast and ovarian cancers. Several studies link BRCA1 to transcriptional regulation, DNA repair, apoptosis and growth/tumor suppression. BRCA1 associates with p53 and stimulates transcription in both p53 dependent and p53-independent manners. BRCA1 splice variants BRCA1a (p110) and BRCA1b (p100) associates with CBP/p300 co-activators. Here we show that BRCA1a and BRCA1b proteins stimulate p53-dependent transcription from the p21 WAF1/CIP1 promoter. In addition, the C-terminal second BRCA1 (BRCT) domain is su cient for p53 mediated transactivation of the p21 promoter. Previous studies emphasized the importance of the BRCT domain, which shows homology with p53 binding protein (53BP1), in transcriptional activation, growth inhibition and tumor suppression. Our ®ndings demonstrate an additional function for this domain in protein ± protein interaction and co-activation of p53. We also found that BRCA1a and BRCA1b proteins interact with p53 in vitro and in vivo. The p53 interaction domain of BRCA1a/1b maps, in vitro, to the second BRCT domain (aa 1760 ± 1863). The BRCT domain binds to the central domain of p53 which is required for sequence speci®c DNA binding. These results demonstrate for the ®rst time the presence of a second p53 interaction domain in BRCA1 proteins and suggests that BRCA1a and BRCA1b proteins, like BRCA1, function as p53 co-activators. This BRCT domain also binds in vitro to CBP. These results suggest that one of the mechanisms by which BRCA1 proteins function is through recruitment of CBP/p300 associated HAT/FAT activity for acetylation of p53 to speci®c promoters resulting in transcriptional activation.

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confidence: 99%

The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter

et al. 1999

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“…An increasing body of results also shows that hTAF II 28, hTAF II 135, and hTAF II 105 can act as specific transcriptional coactivators in mammalian cells. Expression of hTAF II 135 specifically potentiates activation by the liganddependent activation function 2 (AF-2) of the nuclear receptors (NRs) for all-trans retinoic acid (retinoic acid receptor), thyroid hormone (thyroid hormone receptor), and vitamin D 3 (vitamin D 3 receptor [VDR]) (24).…”

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confidence: 99%

“…Expression of hTAF II 135 specifically potentiates activation by the liganddependent activation function 2 (AF-2) of the nuclear receptors (NRs) for all-trans retinoic acid (retinoic acid receptor), thyroid hormone (thyroid hormone receptor), and vitamin D 3 (vitamin D 3 receptor [VDR]) (24). Distinct domains of hTAF II 135 interact specifically with Sp1, CREB, and E1A, and coexpression of the TAF II 135 domains with which these activators interact has a dominant negative effect on their activity (23,28,33,36).…”

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Synergistic Transcriptional Activation by TATA-Binding Protein and hTAF_II28 Requires Specific Amino Acids of the hTAF_II28 Histone Fold

Lavigne

Gangloff

et al. 1999

Molecular and Cellular Biology

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Coexpression of the human TATA-binding protein (TBP)-associated factor 28 (hTAF II 28) with the alteredspecificity mutant TBP spm3 synergistically enhances transcriptional activation by the activation function 2 of the nuclear receptors (NRs) for estrogen and vitamin D 3 from a reporter plasmid containing a TGTA element in mammalian cells. This synergy is abolished by mutation of specific amino acids in the ␣2-helix of the histone fold in the conserved C-terminal region of hTAF II 28. Critical amino acids are found on both the exposed hydrophilic face of this helix and the hydrophobic interface with TAF II 18. This ␣-helix of hTAF II 28 therefore mediates multiple interactions required for coactivator activity. We further show that mutation of specific residues in the H1 ␣-helix of TBP either reduces or increases interactions with hTAF II 28. The mutations which reduce interactions with hTAF II 28 do not affect functional synergy, whereas the TBP mutation which increases interaction with hTAF II 28 is defective in its ability to synergistically enhance activation by NRs. However, this TBP mutant supports activation by other activators and is thus specifically defective for its ability to synergize with hTAF II 28.The RNA polymerase II transcription factor TFIID is a multiprotein complex composed of the TATA-binding protein (TBP) and a series of TBP-associated factors (TAF II s) (3, 7). Not only are TAF II s components of transcription factor TFIID, but distinct subsets of TAF II s are also components of the SAGA, PCAF, and TFTC complexes (13,14,21,31,40). For human TFIID (hTFIID), cDNAs for 11 hTAF II s have been characterized (10,16,18,24,25).Genetic and biochemical experiments show that some TAF II s are important for promoter recognition and expression of a subset of promoters (15,38,39), while others are more generally required for transcription in Saccharomyces cerevisiae (2,26,27,29 Expression of hTAF II 28 also potentiates ligand-dependent activation by the AF-2s of many NRs, the most dramatic effects being seen with the receptors for 9-cis retinoic acid (retinoid X receptor), estrogen (estrogen receptor [ER]), and the VDR (22). Deletion analysis showed that coactivator activity required amino acids 150 to 179 in the C-terminal domain of hTAF II 28. Subsequent determination of the three-dimensional structure of the hTAF II 28/hTAF II 18 heterodimer at 2.6-Å resolution by X-ray crystallography indicated that these two proteins interact via a histone fold motif present in the C-terminal domain of hTAF II 28 and in the central region of hTAF II 18 (4). Amino acids 150 to 179 required for coactivator activity form the amphipathic ␣2-helix of the hTAF II 28 histone fold. In the hTAF II 28/hTAF II 18 heterodimer, residues on the hydrophobic face of the ␣2-helix make intermolecular contacts with hTAF II 18, while the residues on the mainly hydrophilic solvent-exposed face are available for mediating interactions with other proteins.Although the ability of hTAF II 28 to act as a transcriptional coactivator did no...

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“…Since mutation of Thr69 and Thr71 dramatically reduces the basal activity of the ATF2 N-terminus, these two residues might be essential for the interaction of ATF2 with basal transcription factors. In this respect it is interesting to note that transactivation by the cAMP-inducible transcription factor CREB seems to require interactions of CREB with both CBP (following phosphorylation of CREB on Ser133) and TAFII130 (Nakajima et al, 1997). It might be that also in the case of ATF2 two independent protein-protein interactions are involved in transactivation.…”

Section: Discussionmentioning

confidence: 99%

“…cJun) of phosphorylation of the transcription factors (Chrivia et al, 1993;Kwok et al, 1994;. CBP can also associate with the basal transcription factor TFIIB (Kwok et al, 1994) and with the RNA polymerase II complex (Kee et al, 1996;Nakajima et al, 1997), whereas p300 has been shown to interact either directly or indirectly with the TATA-box-binding protein (TBP) (Abraham et al, 1993). Through their interactions with transcription factors, p300 and CBP are thought to upregulate transcription by recruiting the basal transcription apparatus to p300/CBP responsive promoters.…”

Section: Introductionmentioning

confidence: 99%

The N-terminal transactivation domain of ATF2 is a target for the co-operative activation of the c-jun promoter by p300 and 12S E1A

et al. 1999

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Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors.

Cited by 227 publications

References 28 publications

The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter

The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter

Synergistic Transcriptional Activation by TATA-Binding Protein and hTAF_II28 Requires Specific Amino Acids of the hTAF_II28 Histone Fold

The N-terminal transactivation domain of ATF2 is a target for the co-operative activation of the c-jun promoter by p300 and 12S E1A

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Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors.

Cited by 227 publications

References 28 publications

The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter

The second BRCT domain of BRCA1 proteins interacts with p53 and stimulates transcription from the p21WAF1/CIP1 promoter

Synergistic Transcriptional Activation by TATA-Binding Protein and hTAFII28 Requires Specific Amino Acids of the hTAFII28 Histone Fold

The N-terminal transactivation domain of ATF2 is a target for the co-operative activation of the c-jun promoter by p300 and 12S E1A

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Synergistic Transcriptional Activation by TATA-Binding Protein and hTAF_II28 Requires Specific Amino Acids of the hTAF_II28 Histone Fold