XenopusNF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from theXenopus hsp70promoterin vivo

Li, Qiao; Herrler, Michael; Landsberger, Nicoletta; Kaludov, Nikola; Ogryzko, Vasily; Nakatani, Yoshihiro; Wolffe, Alan P.

doi:10.1093/emboj/17.21.6300

Cited by 182 publications

(167 citation statements)

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“…63 It is worth noting that the HSP70 CCAAT element was subsequently investigated as a canonical NF-Y target by the same group. 91,92 As to the mechanistic details of TA, NF-Y has been shown to (i) promote the DNA binding of neighboring activators, (ii) make contacts with multiple general transcription factors, including TBP (TATA-binding protein) and TAFs (TBP-associated factors), (iii) mediate recruitment of Pol II and (iv) bind multiple coactivators -p300, PCAF, MLL -and be post-translationally modified by some of them. 93 The role of YB-1 in activation appears to be related to ssDNA binding in promoter regions (Stein et al 94 ; reviewed in Eliseeva et al 71 ).…”

Section: Nf-y Is the Sequence-specific Ccaat Factormentioning

confidence: 99%

Targeting the Y/CCAAT box in cancer: YB-1 (YBX1) or NF-Y?

Dolfini

Mantovani

2013

Cell Death Differ

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The Y box is an important sequence motif found in promoters and enhancers containing a CCAAT box -one of the few elements enriched in promoters of large sets of genes overexpressed in cancer. The search for the transcription factor(s) acting on it led to the biochemical purification of the nuclear factor Y (NF-Y) heterotrimer, and to the cloning -through the screening of expression libraries -of Y box-binding protein 1 (YB-1), an oncogene, overexpressed in aggressive tumors and associated with drug resistance. These two factors have been associated with Y/CCAAT-dependent activation of numerous growth-related genes, notably multidrug resistance protein 1. We review two decades of data indicating that NF-Y ultimately acts on Y/CCAAT in cancer cells, a notion recently confirmed by genome-wide data. Other features of YB-1, such as post-transcriptional control of mRNA biology, render it important in cancer biology.

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Section: Nf-y Is the Sequence-specific Ccaat Factormentioning

confidence: 99%

Targeting the Y/CCAAT box in cancer: YB-1 (YBX1) or NF-Y?

Dolfini

Mantovani

2013

Cell Death Differ

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“…An important level of regulation links acetylation levels and NF-Y activity. Functionally, inhibition of HDAC's activity by trichostatin A (TSA) treatment leads to 1) activation of the MDR1 (multidrug resistance promoter; Jin and Scotto, 1998); 2) a dramatic increase in the activity of TGF-␤ II receptor promoter (Park et al, 2002); and 3) activation of the HSP70 promoter in the absence of heat shock in Xenopus oocytes (Li et al, 1998). All these effects are strictly dependent on the presence of the CCAAT boxes.…”

Section: Introductionmentioning

confidence: 99%

“…All these effects are strictly dependent on the presence of the CCAAT boxes. NF-Y interacts with hGCN5 (Currie, 1998), and NF-YB is acetylated in Xenopus by p300, but the consequences of this modification have not been addressed (Li et al, 1998). In vivo studies by chromatin immunoprecipitation on cell cycleregulated promoters highlighted the dynamic behavior of NF-Y and HATs binding during cell cycle progression Salsi et al, 2003;Di Agostino et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Posttranslational Regulation of NF-YA Modulates NF-Y Transcriptional Activity

Manni¹,

Caretti

Artuso³

et al. 2008

MBoC

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Here we show that the levels of NF-YA protein are regulated posttranslationally by ubiquitylation and acetylation. A NF-YA protein carrying four mutated lysines in the C-terminal domain is more stable than the wild-type form, indicating that these lysines are ubiquitylated Two of the lysines are acetylated in vitro by p300, suggesting a competition between ubiquitylation and acetylation of overlapping residues. Interestingly, overexpression of a degradation-resistant NF-YA protein leads to sustained expression of mitotic cyclin complexes and increased cell proliferation, indicating that a tight regulation of NF-YA levels contributes to regulate NF-Y activity. INTRODUCTIONThe CCAAT-binding transcription factor NF-Y is a heteromeric protein composed of three subunits, NF-YA, -YB, and -YC, all necessary for CCAAT binding (Mantovani, 1999). The NF-Y complex supports the basal transcription of a class of regulatory genes responsible for cell cycle progression, among which are mitotic cyclin complexes (Zwicker et al., 1995a,b;Bolognese et al., 1999;Farina et al., 1999;Korner et al., 2001;Gurtner et al., 2003Gurtner et al., , 2008Di Agostino et al., 2006). Knock-out mice clearly demonstrates that NF-Y dependent transcription is essential during early mouse development (Bhattacharya et al., 2003). The NF-Y function in proliferation is also demonstrated by the inhibition of DNA binding by endogenous NF-Y, resulting in retardation of fibroblast growth, which is brought about by overexpression of a dominant negative mutant of the NF-YA subunit (Hu and Maity, 2000). The differential expression of NF-YA, altering NF-Y CCAAT-binding activity, has been observed in several cell lines and tissues both during cell cycle progression and under specific conditions. NF-YA expression is modulated during the cell cycle, being high in G1, further increasing in S, and then decreasing in the G2/M phase (Bolognese et al., 1999). Reduction of NF-YA expression has been reported in IMR-90 fibroblasts after serum deprivation (Chang et al., 1994) and in human monocytes (Marziali et al., 1997). The NF-YA protein is not expressed in terminally differentiated C2C12 muscle cells and adult skeletal muscle tissues (Farina et al., 1999;Gurtner et al., 2003Gurtner et al., , 2008. These observations show that levels of NF-YA dictate the function of the NF-Y complex. Interestingly, control of NF-YA accumulation is posttranscriptional, because NF-YA mRNA is relatively constant in growing and differentiated cells (Bolognese et al., 1999;Farina et al., 1999). Yet, the mechanisms regulating the stability of the NF-YA protein remain unknown.The covalent addition of ubiquitin, a 76-amino acid protein highly conserved among eukaryotes, is an increasingly common posttranslation modification that controls both the expression and the activity of numerous proteins in the eukaryotic cell (Hershko and Ciechanover, 1998;Ciechanover et al., 2000). The ubiquitin-proteasome pathway is composed of the ubiquitin-conjugating system and the 26S proteasome; the latter contain...

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“…The minor-groove-interacting transcription factor NF-Y binds to the MDR1 CCAAT box and orchestrates this activation through the recruitment of the coactivator, PCAF (6). PCAF, a factor involved in chromatin remodeling, in turn mediates transcriptional response through its ability to acetylate histones and possibly NF-Y itself (8). Therefore, NF-Y is a central mediator of MDR1 activation and likely functions, at least in part, by facilitating changes in chromatin structure in response to a variety of inducers.…”

mentioning

confidence: 99%