Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach-1

<p><b>Copyright information:</b></p><p>Taken from "Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach"</p><p>http://www.biomedcentral.com/1471-2199/8/43</p><p>BMC Molecular Biology 2007;8():43-43.</p><p>Published online 23 May 2007</p><p>PMCID:PMC1890296.</p><p></p>s well as at the 5' end and 3' end of these target genes

Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach-3

<p><b>Copyright information:</b></p><p>Taken from "Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach"</p><p>http://www.biomedcentral.com/1471-2199/8/43</p><p>BMC Molecular Biology 2007;8():43-43.</p><p>Published online 23 May 2007</p><p>PMCID:PMC1890296.</p><p></p>ichment of target genes relative to IgG on an agarose gel. (B) Real-time PCR demonstrating the relative enrichment of p63 target genes with p63 antibodies and IgG. Primer sequences utilized are listed in Additional File

Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach-5

<p><b>Copyright information:</b></p><p>Taken from "Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach"</p><p>http://www.biomedcentral.com/1471-2199/8/43</p><p>BMC Molecular Biology 2007;8():43-43.</p><p>Published online 23 May 2007</p><p>PMCID:PMC1890296.</p><p></p>omoter demonstrate high levels of activity when co-transfected with an expression plasmid encoding ΔNp63α in PtK2 cells. Luciferase values were determined and normalized against β-galactosidase values. Corrected luciferase values for cells transfected with empty vector pCMV-HA were set at 1. TK; thymidine kinas

Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach-2

<p><b>Copyright information:</b></p><p>Taken from "Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach"</p><p>http://www.biomedcentral.com/1471-2199/8/43</p><p>BMC Molecular Biology 2007;8():43-43.</p><p>Published online 23 May 2007</p><p>PMCID:PMC1890296.</p><p></p>in Additional File to specifically amplify the target genes. β-Actin serves as a control

Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach-6

<p><b>Copyright information:</b></p><p>Taken from "Novel targets of ΔNp63 in keratinocytes identified by a modified chromatin immunoprecipitation approach"</p><p>http://www.biomedcentral.com/1471-2199/8/43</p><p>BMC Molecular Biology 2007;8():43-43.</p><p>Published online 23 May 2007</p><p>PMCID:PMC1890296.</p><p></p>ck-transfected cells were used as a control. Primer sequences used are listed in Additional File

Ovol1 binds to its own promoter and binding requires the zinc finger domain

<p><b>Copyright information:</b></p><p>Taken from "Ovol1 represses its own transcription by competing with transcription activator c-Myb and by recruiting histone deacetylase activity"</p><p></p><p>Nucleic Acids Research 2007;35(5):1687-1697.</p><p>Published online 20 Feb 2007</p><p>PMCID:PMC1865076.</p><p>© 2007 The Author(s).</p> () Organization of the promoter showing the positions of the proximal () and distal () sites, with their sequences shown below the stick diagram. The transcription start site is +1. Also indicated are the positions of primer sets 1 and 2 used for ChIP assays (see below). () Results of EMSA assays showing binding of recombinant Ovol1 to CCGTTA-containing oligonucleotides (left) and (right). Left panel: lane 1, free probe, lanes 2–4, with increasing amounts (172–688 nM) of recombinant His–Ovol1. Right panel: lanes 1 and 7, free probe; lanes 2–6, with increasing concentrations, (50–431 nM) of recombinant His–Ovol1; lanes 8 and 9, with 156 nM recombinant His–Ovol1 and with and without anti-Ovol1 antibody, respectively. Arrowhead and arrow represent Ovol1–DNA and Ovol1–DNA–antibody complexes, respectively. () Results of EMSA assays on using recombinant full-length and truncated Ovol1 proteins. Oval and arrowhead represent full-length and C-terminal Ovol1–DNA complexes, respectively. Lower bands (indicated by *) are likely due to incompletely translated protein products. () DNase1 footprint of the promoter. The sequence of the footprinted region (−53 to −35) is indicated on the right. The bracket on the left indicates the position of the low-affinity site which is present within the oligonucleotide . () Densitometer tracing of hydroxyl radical footprint of the promoter, with the footprinted nucleotides underlined and its position indicated

Opposing effects of Ovol1 and c-Myb on histone H3 acetylation at the endogenous promoter

<p><b>Copyright information:</b></p><p>Taken from "Ovol1 represses its own transcription by competing with transcription activator c-Myb and by recruiting histone deacetylase activity"</p><p></p><p>Nucleic Acids Research 2007;35(5):1687-1697.</p><p>Published online 20 Feb 2007</p><p>PMCID:PMC1865076.</p><p>© 2007 The Author(s).</p> () Results of ChIP assays showing that c-Myb and Ovol1 occupancy correlates with increased and decreased respectively histone H3 acetylation from the basal level. () Results of quantification of ChIP signals. Error bars were calculated from three independent PCR reactions of a single immunoprecipitate, and results are representative of multiple ChIP experiments. ‘*’ indicates statistically significant ( < 0.003) difference from the untransfected sample