scholarly journals Improvement of the Chromatin Immunoprecipitation (ChIP) Assay by DNA Fragment Size Fractionation

BioTechniques ◽  
2001 ◽  
Vol 31 (4) ◽  
pp. 740-742 ◽  
Author(s):  
Trina A. Johnson ◽  
Heather L. Wilson ◽  
William J. Roesler
Keyword(s):  
Chromatin Immunoprecipitation ◽  
Fragment Size ◽  
Chip Assay ◽  
Size Fractionation ◽  
Dna Fragment

Chromatin immunoprecipitation (ChIP) assay

2009 ◽  
Author(s):  
Zhongfu Ni ◽  
Danny W.-K. Ng ◽  
Jianxin Liu ◽  
Z. Jeffrey Chen
Keyword(s):  
Chromatin Immunoprecipitation ◽  
Chip Assay

scholarly journals ЦАХИЛДАГНЫ ТӨРЛИЙН УРГАМЛЫН ФИЛОГЕНЕТИК ХОЛБОО

2016 ◽  
pp. 25-31
Author(s):  
Х Алтанзул ◽  
Ю Оюунбилэг
Keyword(s):  
Phylogenetic Tree ◽  
Phylogenetic Relationship ◽  
Dna Sequences ◽  
Fragment Size ◽  
Dna Fragment ◽  
Relationship Of

The phylogenetic relationship of eight Iris species (I.flavisimma, I.ventricosa, I.bungei,I.kaempferi, I.tenuifolia, I.lactea, I.tigrida, I.dichotoma) were studied by PCR using six specificprimers (S-523, Z1204R, trnL, trnF and ITS1, ITS4). All species except I.ventricosa wereidentified when using S-523, Z1204R and trnL, trnF primers and the DNA fragment size rangedbetween 500 to 600 bp and 800 bp, respectively. Primers ITS1 and ITS4 produced double bandsin about 500 and 1500 bp to I.bungei, I.kaempferi, and I.lactea species. On the phylogenetic tree, some iris species have close relations based on chloroplastic DNA sequences. The closest relationships showed between I.sanguinea and I.sibirica, I.rutenica and I.uniflora. Also I.tenuifolia, I.ventricosa and I.halophila located on one branch of phylogenetic tree.

Yeast Chromatin Immunoprecipitation (ChIP) Assay

2007 ◽  
Vol 2007 (1) ◽  
pp. pdb.prot4642-pdb.prot4642
Author(s):  
W. P. Tansey
Keyword(s):  
Chromatin Immunoprecipitation ◽  
Chip Assay

scholarly journals The Autoregulatory and Transactivating Functions of the Human Cytomegalovirus IE86 Protein Use Independent Mechanisms for Promoter Binding

2007 ◽  
Vol 81 (11) ◽  
pp. 5807-5818 ◽  
Author(s):  
Dustin T. Petrik ◽  
Kimberly P. Schmitt ◽  
Mark F. Stinski
Keyword(s):  
Human Cytomegalovirus ◽  
Protein Interactions ◽  
Chromatin Immunoprecipitation ◽  
Viral Gene Expression ◽  
Artificial Chromosome ◽  
Viral Gene ◽  
Chip Assay ◽  
Protein Protein Interactions ◽  
Multiple Sequence ◽  
Viral Genes

ABSTRACT The functions of the human cytomegalovirus (HCMV) IE86 protein are paradoxical, as it can both activate and repress viral gene expression through interaction with the promoter region. Although the mechanism for these functions is not clearly defined, it appears that a combination of direct DNA binding and protein-protein interactions is involved. Multiple sequence alignment of several HCMV IE86 homologs reveals that the amino acids 534LPIYE538 are conserved between all primate and nonprimate CMVs. In the context of a bacterial artificial chromosome (BAC), mutation of both P535 and Y537 to alanines (P535A/Y537A) results in a nonviable BAC. The defective HCMV BAC does not undergo DNA replication, although the P535A/Y537A mutant IE86 protein appears to be stably expressed. The P535A/Y537A mutant IE86 protein is able to negatively autoregulate transcription from the major immediate-early (MIE) promoter and was recruited to the MIE promoter in a chromatin immunoprecipitation (ChIP) assay. However, the P535A/Y537A mutant IE86 protein was unable to transactivate early viral genes and was not recruited to the early viral UL4 and UL112 promoters in a ChIP assay. From these data, we conclude that the transactivation and repressive functions of the HCMV IE86 protein can be separated and must occur through independent mechanisms.

scholarly journals Extrapolation of the DNA Fragment-Size Distribution after High-Dose Irradiation to Predict Effects at Low Doses

2001 ◽  
Vol 156 (5) ◽  
pp. 594-597 ◽  
Author(s):  
A. L. Ponomarev ◽  
F. A. Cucinotta ◽  
R. K. Sachs ◽  
D. J. Brenner ◽  
L. E. Peterson
Keyword(s):  
Size Distribution ◽  
Fragment Size ◽  
High Dose ◽  
Low Doses ◽  
Fragment Size Distribution ◽  
Dose Irradiation ◽  
Dna Fragment

scholarly journals Analysis of cell‐free circulating DNA fragment size and level in patients with lumbar canal stenosis

JOR Spine ◽  
2021 ◽  
Author(s):  
Akihiko Hiyama ◽  
Daisuke Sakai ◽  
Satoshi Nomura ◽  
Hiroyuki Katoh ◽  
Masahiko Watanabe
Keyword(s):  
Fragment Size ◽  
Circulating Dna ◽  
Lumbar Canal Stenosis ◽  
Canal Stenosis ◽  
Dna Fragment ◽  
Free Circulating Dna

scholarly journals PRMT5 Prevents Cardiomyocyte Hypertrophy via Symmetric Dimethylating HoxA9 and Repressing HoxA9 Expression

2020 ◽  
Vol 11 ◽  
Author(s):  
Sidong Cai ◽  
Rong Liu ◽  
Panxia Wang ◽  
Jingyan Li ◽  
Tingting Xie ◽  
...  
Keyword(s):  
Chromatin Immunoprecipitation ◽  
Adrenergic Receptor ◽  
Receptor Agonist ◽  
Therapeutic Strategies ◽  
Cardiomyocyte Hypertrophy ◽  
Chip Assay ◽  
Loss Of Function ◽  
Arginine Methyltransferase ◽  
Physical Interactions ◽  
Adrenergic Receptor Agonist

The present study reveals a link between protein arginine methyltransferase 5 (PRMT5) and Homebox A9 (HoxA9) in the regulation of cardiomyocyte hypertrophy. In cardiomyocyte hypertrophy induced by β-adrenergic receptor agonist isoprenaline (ISO), PRMT5 expression was decreased while HoxA9 was upregulated. Silencing of PRMT5 or inhibition of PRMT5 by its pharmacological inhibitor EPZ augmented the expressions of cardiomyocyte hypertrophic genes brain natriuretic peptide (BNP) and β-Myosin Heavy Chain (β-MHC), whereas overexpression of PRMT5 inhibited ISO-induced cardiomyocyte hypertrophy, suggesting that PRMT5 ameliorates cardiomyocyte hypertrophy. On the contrary, HoxA9 promoted cardiomyocyte hypertrophy, as implied by the gain-of-function and loss-of-function experiments. HoxA9 was involved in the regulation of PRMT5 in cardiomyocyte hypertrophy, since HoxA9 knockdown prevented si-RPMT5-induced cardiomyocyte hypertrophy, and HoxA9 expression impaired the anti-hypertrophic effect of PRMT5. Co-immunoprecipitation experiments revealed that there were physical interactions between PRMT5 and HoxA9. The symmetric dimethylation level of HoxA9 was decreased by ISO or EPZ treatment, suggesting that HoxA9 is methylated by PRMT5. Additionally, PRMT5 repressed the expression of HoxA9. Chromatin immunoprecipitation (ChIP) assay demonstrated that HoxA9 could bind to the promoter of BNP, and that this binding affinity was further enhanced by ISO or EPZ. In conclusion, this study suggests that PRMT5 symmetric dimethylates HoxA9 and represses HoxA9 expression, thus impairing its binding to BNP promoter and ultimately protecting against cardiomyocyte hypertrophy. These findings provide a novel insight of the mechanism underlying the cardiac protective effect of PRMT5, and suggest potential therapeutic strategies of PRMT5 activation or HoxA9 inhibition in treatment of cardiac hypertrophy.

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