Project description:Chromatin immunoprecipitation of Set3 complex applied with tilling array chip ( ChIP on chip of either Set3-TAP or Snt1-TAP) analysis demonstrated that the genome-wide localization of Set3 complex in Saccharomyces cerevisiae
Project description:Chromatin immunoprecipitation of Sir3 applied with tilling array chip ( ChIP on chip of Sir3) analysis demonstrated that Changes of conventional and dynamical Genome-wide localization of Sir3 in Saccharomyces cerevisiae during different growth stages
Project description:To search for the functional “m6A readers” specifically in the context of Drosophila early embryos, we incubated m6A-modified or unmodified RNA probes with cytosolic lysates from early embryos, and performed immunoprecipitation experiments followed by mass spectrometry analysis. We found that Drosophila FMRP (FMR1) was highly abundant in complexes immuno-precipitated by the m6A-modified probe. We performed data-independent acquisition (DIA) quantitative proteomics on the wild type and fmr1 maternal mutant embryos at multiple developmental stages, including 0-1 h, 2-3 h, and 5-6 h stages. To screen the FMR1-associated partners, we collected the 2–3-hour embryos and performed immunoprecipitation using the anti-Drosophila FMR1 antibody, followed by mass spectrometric analysis.
Project description:O-acetyl-ADP-ribose (AAR) is a small metabolic molecule that is generated during NAD-dependent deacetylation by Sir2. Sir2 regulates gene expression, DNA repair, and genome stability. chromatin affinity-precipitation (ChAP) method was used to detect the chromatin fragments at which small molecules interact with binding partners. Chromatin immunoprecipitation of Sir3 and of Sir2, respectively, applied with tilling array chip (ChIP on chip of Sir3 and of Sir2, respectively) and Chromatin affinity-precipitation of AAR applied with tilling array chip (ChAP on chip of AAR ) analysis demonstrated that an extended spreading of Sir3 and of AAR, but not Sir2 in Saccharomyces cerevisiae Ysa1 deleted cells compared with those in wild type cells
Project description:Chromatin immunoprecipitation of Snt1, of PolII, and of H3K4me2, respectively, applied with tilling array chip (ChIP on chip of Snt1, of PolII, and of H3K4me2, respectively) analysis demonstrated that a compared genomic occupancy of Snt1, of PolII, and of H3K4me2 in Saccharomyces cerevisiae wild type cells compared anong those in Hst1 deleted, Hos2 deleted and Hst2 & Hos2 double deleted cells
Project description:Chromatin immunoprecipitation of Set3, of PolII, and of H3K4me2, respectively, applied with tilling array chip (ChIP on chip of Set3, of PolII, and of H3K4me2, respectively) analysis demonstrated that a compared genomic occupancy of Set3, of PolII, and of H3K4me2 in Saccharomyces cerevisiae wild type cells compared anong those in Hst1 deleted, Hos2 deleted and Hst2 & Hos2 double deleted cells
Project description:To understand the role of MiT in Drosophila, we set out to identify critical gene targets by looking at changes in the WT transcriptome induced by either gain or loss of MiT function. Mutant hindgut and malpighian tubules provided loss-of function tissue and nub-Gal4-driven expression of MiT in the wing epithelium was used for gain-of-function. In the wing disc experiment, 543 genes were upregulated by exogenous MiT, and 359 genes were downregulated (>1.4 fold; P value < 0.01). In the larval HG+MT, 897 genes were downregulated and 898 were upregulated (>1.4 fold; P value < 0.01) after MiT. Among these genes, 85 were both upregulated in wing discs and downregulated in mutant HG+MT, and are the common genes that regulated by MiT in both tissues.
Project description:To identify Aub function in mRNA regulation in the Drosophila embryo, we have performed mass spectrometry analysis of Aub interactors, following immunoprecipitation of GFP-Aub in 0-2 hour-embryos. Immunoprecipitation of GFP alone was used as negative control. Because Aub accumulates at high levels in the germ plasm, GFP-Aub immunoprecipitation was also performed in oskar mutant embryos that do not assemble the germ plasm. Proteins coprecipitating with GFP-Aub were similar in wild-type and oskar mutant embryos. Translation factors were enriched among proteins coprecipitating with Aub.