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Related Concept Videos

Eukaryotic Transcription Activators02:42

Eukaryotic Transcription Activators

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Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
The binding domains are capable of recognizing and interacting with regulatory sequences on the DNA. These...
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tRNA Activation02:26

tRNA Activation

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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RNA Polymerase II Accessory Proteins02:36

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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Epigenetic Regulation01:37

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Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
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Translesion DNA Polymerases02:10

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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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Related Experiment Video

Updated: Aug 20, 2025

Continuous Fluorescence-Based Endonuclease-Coupled DNA Methylation Assay to Screen for DNA Methyltransferase Inhibitors
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Structural basis for activation of DNMT1.

Amika Kikuchi1, Hiroki Onoda1,2, Kosuke Yamaguchi3

  • 1Structural Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan.

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|November 22, 2022
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Summary

Researchers uncovered how DNA methyltransferase 1 (DNMT1) is activated. A key linker region repositions domains, enabling DNMT1 to maintain DNA methylation, crucial for genomic stability and drug design.

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Immunostaining for DNA Modifications: Computational Analysis of Confocal Images
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In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 Ehmeth Enzyme
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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Epigenetics

Background:

  • DNA methyltransferase 1 (DNMT1) is vital for maintaining genomic DNA methylation patterns.
  • The precise regulatory mechanisms governing DNMT1 activity remain incompletely understood.
  • DNMT1 function is influenced by interactions with DNA and histone modifications.

Purpose of the Study:

  • To elucidate the structural basis for human DNMT1 activation.
  • To investigate the role of specific protein domains and linkers in DNMT1 regulation.
  • To provide a mechanistic understanding of DNMT1 activation by its natural activators.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the structure of human DNMT1.
  • The structure was resolved in complex with hemimethylated DNA and ubiquitinated histone H3.
  • Analysis focused on domain interactions and conformational changes upon activation.

Main Results:

  • A previously uncharacterized linker region between the RFTS and CXXC domains is critical for DNMT1 activation.
  • This linker contains a conserved alpha-helix that interacts with a 'Toggle' pocket, displacing an inhibitory linker.
  • Activation involves large-scale reorganization of the RFTS and CXXC domains, leading to the DNA Recognition Helix adopting an active conformation.

Conclusions:

  • The study provides a detailed mechanistic explanation for DNMT1 activation.
  • The findings reveal how specific structural elements facilitate the enzyme's transition to its active state.
  • This structural insight has implications for fundamental research in epigenetics and for the development of targeted therapeutics.