Irradiation modulates association of NF-Y with histone-modifying cofactors PCAF and HDAC

Peng, Yang; Stewart, Denise; Li, W; Hawkins, Meredith; Kulak, Stephen C.; Ballermann, Barbara J.; Jahroudi, Nadia

doi:10.1038/sj.onc.1210565

Cited by 32 publications

(27 citation statements)

References 22 publications

(31 reference statements)

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“…This is consistent with the fact that the architecture of the CBF-DNA assembly is very similar to that of the histone H2A/ H2B-DNA assembly in the nucleosome (45), suggesting a possible regulatory role as an H2A/H2B-like variant (46). Moreover, CBF interacts with histone acetyltransferases, suggesting that CBF may play an important role in local chromatin modulation by means of histone modification (47)(48)(49)(50)(51).…”

Section: Discussionsupporting

confidence: 69%

Antagonistic Controls of Chromatin and mRNA Start Site Selection by Tup Family Corepressors and the CCAAT-Binding Factor

Asada

Takemata

Hoffman

et al. 2015

Molecular and Cellular Biology

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The Tup family corepressors contribute to critical cellular responses, such as the stress response and differentiation, presumably by inducing repressive chromatin, though the precise repression mechanism remains to be elucidated. E ukaryotic chromosomal DNA is packaged in a highly organized and condensed chromatin structure. Many DNA-associated reactions, including DNA damage repair, replication, recombination, and transcription, are regulated by the chromatin structure (1, 2). The chromatin structure is modulated by two distinct classes of regulators, histone modification enzymes and ATP-dependent chromatin remodeling factors (3, 4). Such regulatory components are recruited by two types of cis-acting regulatory factors, transcriptional activators and repressors. Transcriptional activators and repressors bind to cis-acting elements to activate and repress transcription, respectively, by affecting the chromatin structure and regulating RNA polymerase II accumulation in the promoter region (5-7). These transcriptional regulators also interact with coactivators and corepressors to regulate gene expression (8, 9). The Tup family transcriptional corepressors are conserved between yeast and humans and regulate gene expression during the stress response and cellular differentiation (10, 11). Saccharomyces cerevisiae Tup1 represses some genes regulated by cell type, glucose, oxidative stress, DNA damage, and other cellular stress responses (12, 13). Tup1 represses the expression of genes via distinct mechanisms: by establishing a repressive chromatin structure around the target gene promoter, by recruiting histone deacetylases, and by directly interfering with the general transcription machinery (14-18). Two Tup1 orthologs in Schizosaccharomyces pombe, Tup11 and Tup12 (Tup11/12), regulate multiple stress-responsive genes, including the fbp1 ϩ and cta3 ϩ genes, to provide stress specificity (19,20). However, the precise molecular mechanisms of Tup1 family proteins in gene repression have not been fully uncovered.The fbp1 ϩ gene encodes fructose-1,6-bisphosphatase and is robustly induced upon glucose starvation (21,22). fbp1 ϩ expression is strictly repressed by Tup11/12 and activated by the transcriptional activators Atf1, Rst2, and Php5 (23-26). Atf1, a bZIP protein, is regulated through phosphorylation by the mitogen-activated protein kinase pathway (27-29), while Rst2, a C 2 H 2 Zn finger-type protein, is under the regulation of the protein kinase A pathway (23, 30). Php5, a component of the S. pombe CCAATbinding factor (CBF; also known as NF-Y) that possesses a histone hold domain, forms a complex with Php2/Php3 and contributes to cyc1 ϩ transcription (31, 32). In addition, two cis-acting elements required for fbp1 ϩ transcription have been identified (33). Upstream activation sequence 1 (UAS1) contains a cyclic AMP response element (CRE) and is the binding site for Atf1 and its binding partner, Pcr1 (34), while UAS2 resembles the S. cerevisiae stress response element (STRE) and serves as the binding site for Rst2 (...

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Section: Discussionsupporting

confidence: 69%

Antagonistic Controls of Chromatin and mRNA Start Site Selection by Tup Family Corepressors and the CCAAT-Binding Factor

Asada

Takemata

Hoffman

et al. 2015

Molecular and Cellular Biology

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“…Further, transcription factors other than NFY and Sp1 could also be involved in the binding and recruitment of HAT to the FPGS promoter. For instance, interactions between NFY and HAT proteins such as the coactivator p300 [66][67][68][69][70][71] have been described previously. This dual mechanism of regulation involving both HATs and HDACs has recently been shown for the TbRII promoter in which transforming growth factor-b expression was found to be induced both by trichostatin-A, a HDACI, and by acetylation of Sp1 after recruitment of PCAF/ p300 to an Sp1/NFY complex.…”

Section: Discussionmentioning

confidence: 99%

Histone deacetylase inhibitors induce FPGS mRNA expression and intracellular accumulation of long-chain methotrexate polyglutamates in childhood acute lymphoblastic leukemia: implications for combination therapy

et al. 2010

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Children with acute lymphoblastic leukemia (ALL) diagnosed with resistant phenotypes, and those who relapse, have a dismal prognosis for cure. The antifolate methotrexate (MTX), a universal component of ALL therapies, is metabolized by folylpoly-c-glutamate synthetase (FPGS) into long-chain polyglutamates (MTX-PG 3À7 ), resulting in enhanced cytotoxicity from prolonged inhibition of dihydrofolate reductase (DHFR) and thymidylate synthetase (TS). Using DNaseI assays, we identified a hypersensitive site upstream from exon-1, suggesting chromatin remodeling could alter FPGS expression. We demonstrated that histone deacetylase-1 (HDAC1) is recruited by NFY and Sp1 transcription factors to the FPGS promoter in ALL cell lines. We examined the effect of histone deacetylase inhibitors (HDACIs) sodium butyrate and suberoylanilide hydroxamic acid (SAHA) on the expression of FPGS and other folate-related genes. HDACIs increased FPGS mRNA expression by 2-to 5-fold, whereas DHFR and TS mRNA expression was decreased. Combination treatment with MTX plus SAHA significantly increased cytotoxicity and apoptosis in B-and T-ALL cell lines as compared with each drug alone (CIp0.8). SAHA increased the intracellular accumulation of long-chain MTX-PG 3À7 . Therefore, HDACI-induced FPGS expression increases the accumulation of MTX-PG 3À7 and cytotoxicity in ALL cell lines, which is potentiated by DHFR and TS downregulation. The synergism exhibited by the combination of MTX and SAHA warrants clinical testing in ALL patients.

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“…Several studies showed that NF-Y associates with KAT2A/B [53][54][55][56][57] and with histone-fold TAFs, 58 which are part of the complexes; it remains to be seen whether there are direct interactions with the subunits of the SAGA and ATAC complexes analyzed here.…”

confidence: 99%

NF-Y affects histone acetylation and H2A.Z deposition in cell cycle promoters

Gatta¹,

Mantovani²

2011

Epigenetics

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Irradiation modulates association of NF-Y with histone-modifying cofactors PCAF and HDAC

Cited by 32 publications

References 22 publications

Antagonistic Controls of Chromatin and mRNA Start Site Selection by Tup Family Corepressors and the CCAAT-Binding Factor

Antagonistic Controls of Chromatin and mRNA Start Site Selection by Tup Family Corepressors and the CCAAT-Binding Factor

Histone deacetylase inhibitors induce FPGS mRNA expression and intracellular accumulation of long-chain methotrexate polyglutamates in childhood acute lymphoblastic leukemia: implications for combination therapy

NF-Y affects histone acetylation and H2A.Z deposition in cell cycle promoters

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