Acetyltransferase machinery conserved in p300/CBP-family proteins

Yuan, Lei; Giordano, Antonio

doi:10.1038/sj.onc.1205283

Cited by 49 publications

(37 citation statements)

References 55 publications

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“…HsfB1 binding in close vicinity to an acidic activator leads to cooperative recruitment of components of the transcriptional machinery. Evidently, the GRGKMMK motif in the C terminus of HsfB1 plays a central role for its coactivator function because it serves as binding site for the plant CBP orthologs HAC1 to HAC5 recently identified by sequence comparison in the Arabidopsis genome (Bordoli et al, 2001;Yuan and Giordano, 2002). We have provided evidence that AtHAC1 and mammalian CBP exert a strong and specific stimulatory effect on gene activation in plant cells ( Figure 4).…”

Section: The Histone-like Motif Of Hsfb1 and The Role Of Hac1/cbpmentioning

confidence: 75%

“…Five CBP-like proteins (HAC1 to HAC5) were identified recently in Arabidopsis (Bordoli et al, 2001;Yuan and Giordano, 2002). All contain the most conserved central parts with the three Zn finger (C/H1 to C/H3) and the embedded HAT domains (see block diagrams in Figure 4A).…”

Section: Synergism Results From Corecruitment Of Hac1/cbpmentioning

confidence: 99%

“…The intriguing role of the GRGK motif both in histones and HsfB1 led us to investigate the influence of CBP in reporter assays with coexpression of HsfA1 and HsfB1. In animal cells, CBP is a 300-kD global coactivator with histone acetyl transferase (HAT) activity, interacting with many transcription factors either bound to the N-terminal domain or to the CTD of the protein (Sterner and Berger, 2000;Bannister and Miska, 2000;Chan and LaThangue, 2001;Yuan and Giordano, 2002). To evaluate the synergistic activation of GUS expression, tobacco protoplasts were transformed and tested in the four standard combinations of reporter and activators ( Figure 1B, arrows).…”

Section: Synergism Results From Corecruitment Of Hac1/cbpmentioning

confidence: 99%

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Tomato Heat Stress Transcription Factor HsfB1 Represents a Novel Type of General Transcription Coactivator with a Histone-Like Motif Interacting with the Plant CREB Binding Protein Ortholog HAC1[W]

et al. 2004

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In contrast with the class A heat stress transcription factors (HSFs) of plants, a considerable number of HSFs assigned to classes B and C have no evident function as transcription activators on their own. However, in the following article, we provide evidence that tomato (Lycopersicon peruvianum) HsfB1 represents a novel type of coactivator cooperating with class A HSFs (e.g., with tomato HsfA1). Provided the appropriate promoter architecture, the two HSFs assemble into an enhanceosome-like complex, resulting in strong synergistic activation of reporter gene expression. Moreover, HsfB1 also cooperates in a similar manner with other activators, for example, with the ASF1/2 enhancer binding proteins of the 35S promoter of Cauliflower mosaic virus or with yet unidentified activators controlling housekeeping gene expression. By these effects, HsfB1 may help to maintain and/or restore expression of certain viral or housekeeping genes during ongoing heat stress. The coactivator function of HsfB1 depends on a histone-like motif in its C-terminal domain with an indispensable Lys residue in the center (GRGKMMK). This motif is required for recruitment of the plant CREB binding protein (CBP) ortholog HAC1. HsfA1, HsfB1, and HAC1/CBP form ternary complexes in vitro and in vivo with markedly enhanced efficiency in promoter recognition and transcription activation in plant and mammalian (COS7) cells. Using small interfering RNA–mediated knock down of HAC1 expression in Arabidopsis thaliana mesophyll protoplasts, the crucial role for the coactivator function of HsfB1 was confirmed.

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Section: The Histone-like Motif Of Hsfb1 and The Role Of Hac1/cbpmentioning

confidence: 75%

Section: Synergism Results From Corecruitment Of Hac1/cbpmentioning

confidence: 99%

Section: Synergism Results From Corecruitment Of Hac1/cbpmentioning

confidence: 99%

See 1 more Smart Citation

Tomato Heat Stress Transcription Factor HsfB1 Represents a Novel Type of General Transcription Coactivator with a Histone-Like Motif Interacting with the Plant CREB Binding Protein Ortholog HAC1[W]

et al. 2004

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“…Several versions of the Taz2 peptide of varying lengths derived from the human p300 protein were prepared for crystallographic studies: Taz2(1723-1812) and Taz2(1723Taz2( -1816 correspond to an evolutionarily conserved domain (Yuan & Giordano, 2002), whereas the longer construct Taz2(1723-1836) was designed based on secondary-structure predictions. To prevent misfolding and/or aggregation arising from oxidation, the four Cys residues which are not involved in coordination of the zinc ions (Cys1738, Cys1746, Cys1789 and Cys1790) were mutated to alanines using the QuikChange mutagenesis kit (Stratagene, La Jolla, California, USA).…”

Section: Protein Production and Crystallizationmentioning

confidence: 99%

Structure of the Taz2 domain of p300: insights into ligand binding

Miller

Dauter

Cherry³

et al. 2009

Acta Crystallogr D Biol Crystallogr

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CBP and its paralog p300 are histone acetyl transferases that regulate gene expression by interacting with multiple transcription factors via specialized domains. The structure of a segment of human p300 protein (residues 1723-1836) corresponding to the extended zinc-binding Taz2 domain has been investigated. The crystal structure was solved by the SAD approach utilizing the anomalous diffraction signal of the bound Zn ions. The structure comprises an atypical helical bundle stabilized by three Zn ions and closely resembles the solution structures determined previously for shorter peptides. Residues 1813-1834 from the current construct form a helical extension of the C-terminal helix and make extensive crystalcontact interactions with the peptide-binding site of Taz2, providing additional insights into the mechanism of the recognition of diverse transactivation domains (TADs) by Taz2. On the basis of these results and molecular modeling, a hypothetical model of the binding of phosphorylated p53 TAD1 to Taz2 has been proposed.

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“…The steroid receptor coactivator proteins have receptor interaction domains containing LXXLL motifs that contact the ligand-binding domains (13). The p300 and CBP proteins are histone acetyltransferases (HATs) that mediate the acetylation of nucleosomal histones, a covalent modification generally associated with the enhancement of transcription (reviewed in references 14,15).…”

mentioning

confidence: 99%

Human ADA3 Binds to Estrogen Receptor (ER) and Functions As a Coactivator for ER-mediated Transactivation

Meng

Zhao²,

Nag³

et al. 2004

Journal of Biological Chemistry

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We have recently identified the hADA3 protein, the human homologue of yeast transcriptional coactivator yADA3, as a novel HPV16 E6 target. Using ectopic expression approaches, we further demonstrated that hADA3 directly binds to the 9-cis retinoic acid receptors ␣ and ␤, and functions as a coactivator for retinoid receptor-mediated transcriptional activation. Here, we examined the role of endogenous hADA3 as a coactivator for estrogen receptor (ER), an important member of the nuclear hormone receptor superfamily. We show that ADA3 directly interacts with ER␣ and ER␤. Using the chromatin immunoprecipitation assay, we also show that hADA3 is a component of the activator complexes bound to the native ER response element within the promoter of the estrogen-responsive gene pS2. Furthermore, using an ER response element-luciferase reporter, we show that overexpression of ADA3 enhances the ER␣-and ER␤-mediated sequence-specific transactivation. Reverse transcription-PCR analysis showed an ADA3-mediated increase in estrogen-induced expression of the endogenous pS2 gene. More importantly, using RNA interference against hADA3, we demonstrate that inhibition of endogenous hADA3 inhibited ER-mediated transactivation and the estrogeninduced increase in the expression of pS2, cathepsin D, and progesterone receptor, three widely known ERresponsive genes. The HPV E6 protein, by targeting hADA3 for degradation, inhibited the ER␣-mediated transactivation and the protein expression of ER target genes. Thus, our results demonstrate that ADA3 directly binds to human estrogen receptor and enhances the transcription of ER-responsive genes, suggesting a broader role of mammalian hADA3 as a coactivator of nuclear hormone receptors and the potential role of these pathways in HPV oncogenesis.

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Acetyltransferase machinery conserved in p300/CBP-family proteins

Cited by 49 publications

References 55 publications

Tomato Heat Stress Transcription Factor HsfB1 Represents a Novel Type of General Transcription Coactivator with a Histone-Like Motif Interacting with the Plant CREB Binding Protein Ortholog HAC1[W]

Tomato Heat Stress Transcription Factor HsfB1 Represents a Novel Type of General Transcription Coactivator with a Histone-Like Motif Interacting with the Plant CREB Binding Protein Ortholog HAC1[W]

Structure of the Taz2 domain of p300: insights into ligand binding

Human ADA3 Binds to Estrogen Receptor (ER) and Functions As a Coactivator for ER-mediated Transactivation

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