A new reagent for the oxidative cleavage of DNA, (1,4,7-trimethyl-1, 4,7-triazacyclononane)iron(III) chloride was recently introduced. We have determined the utility of this reagent for detecting protein-DNA interactions within two types of complexes. Interestingly, we find that the rates of DNA cleavage by this reagent are differentially affected by the two classes of protein-DNA interactons studied. We find that the rate of DNA cleavage by this reagent is relatively unaffected by the non-sequence-specific histone-DNA interactions within a nucleosome complex. Conversely, a clear footprint pattern is obtained with two different DNA sequence-specific protein-DNA complexes. The results suggest that (1,4,7-trimethyl-1,4,7-triazacyclononane)iron(III) chloride will be a useful reagent to probe trans -acting-factor-DNA interactions within a chromatin environment. Differences between these two types of protein-DNA interactions, which might account for this observation, are discussed.
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http://dx.doi.org/10.1093/nar/26.9.2086 | DOI Listing |
Nat Commun
January 2025
Key Laboratory of Seed Innovation, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Mediator25 (MED25) has been ascribed as a signal-processing and -integrating center that controls jasmonate (JA)-induced and MYC2-dependent transcriptional output. A better understanding of the regulation of MED25 stability will undoubtedly advance our knowledge of the precise regulation of JA signaling-related transcriptional output. Here, we report that Arabidopsis MED16 activates JA-responsive gene expression by promoting MED25 stability.
View Article and Find Full Text PDFMethods Cell Biol
January 2025
Department of Medical Biochemistry and Molecular Biology and Immunology, Medical School, Virgen Macarena University Hospital, University of Seville, Seville, Spain; Cancer Division, Faculty of medicine, Imperial college London, United Kingdom.
Histones are essential nuclear proteins that package eukaryotic DNA into chromosomes, play a vital role in gene regulation, DNA replication, DNA repair and chromosome condensation. Understanding histone modifications is crucial for grasping biological and disease-related processes. Specific alterations in histone modifications serve as sensitive and selective biomarkers for conditions like cancer, impacting both tumor and immune cells and affecting their interactions.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai 200032, China. Electronic address:
Proto-oncogene RET is overexpressed in many cancers, and its expression level is positively related to the size and malignancy of the tumors. Effective inhibition of its overexpression can be used to potentially treat cancers. A guanine-rich GC-boxes (I-V) sequence in its promoter region folds into noncanonical G-quadruplex (G4) DNA structures, negatively regulating its expression by interactions with small molecules.
View Article and Find Full Text PDFVet Microbiol
December 2024
Chongqing Academy of Animal Sciences, Chongqing 402460, China; Southwest University, College of Veterinary Medicine, Chongqing 400715, China; Department of Infectious Diseases, The First Affiliated Hospital of Anhui Medical University, Hefei 230022, China; State Key Laboratory of Silkworm Genome Biology, Chongqing 400715, China. Electronic address:
lncRNAs play important regulatory roles in almost every aspect of physiological processes. However, the mechanisms by which animal-encoded lncRNAs regulate the interaction of viral infection with host antiviral immunity are unknown. To explore the mechanisms of lncRNA regulation of SVV infection and interferon responses.
View Article and Find Full Text PDFRSC Chem Biol
January 2025
Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences Flemingovo n. 2 Prague 6 Czechia
The LutR protein represses the transcription of genes encoding enzymes for the utilization of l-lactate in through binding to a specific DNA region. In this study, we employed oligonucleotide probes modified by viscosity-sensitive tetramethylated thiophene-BODIPY fluorophores to investigate the impact of selected metabolites on the LutR-DNA complex. Our goal was to identify the effector molecule whose binding alters the protein-DNA affinity, thereby enabling gene transcription.
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