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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Epigenetic Regulation01:37

Epigenetic Regulation

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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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Epigenetic Regulation01:46

Epigenetic Regulation

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Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
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Spreading of Chromatin Modifications02:25

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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RNA Editing02:23

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RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
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Immunostaining for DNA Modifications: Computational Analysis of Confocal Images
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Editing and methylation at a single site by functionally interdependent activities.

Mary Anne T Rubio1, Kirk W Gaston1,2, Katherine M McKenney1

  • 1Department of Microbiology, Ohio State Biochemistry Program and The Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA.

Nature
|February 24, 2017
PubMed
Summary
This summary is machine-generated.

Chemical modifications in nucleic acids are crucial but often poorly understood. This study reveals that cytosine methylation is a prerequisite for deamination in Trypanosoma brucei tRNA, explaining genome stability.

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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
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An Engineered Split-TET2 Enzyme for Chemical-inducible DNA Hydroxymethylation and Epigenetic Remodeling
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Nucleic acids possess over 100 known chemical modifications, affecting bases and sugars.
  • The biosynthetic pathways for most nucleic acid modifications remain largely unelucidated.
  • Enzyme reconstitution in vitro is challenging, suggesting complex modification pathways or interdependence.

Purpose of the Study:

  • To investigate the mechanism of tRNA cytosine-to-uridine editing in eukaryotes.
  • To elucidate the role of modification interdependence in enzymatic activity.
  • To understand how Trypanosoma brucei maintains genome integrity despite possessing mutagenic deaminases.

Main Methods:

  • Investigated the modification of cytosine 32 in Trypanosoma brucei tRNAThr.
  • Reconstituted enzyme activity in vitro using purified components, including TRM140 methyltransferase and ADAT2/3 deaminase.
  • Co-expression of methyltransferase and deaminase to assess enzyme activity and mutagenicity.

Main Results:

  • Cytosine 32 in T. brucei tRNAThr is methylated to 3-methylcytosine (m3C) by TRM140.
  • m3C serves as a prerequisite for subsequent deamination to 3-methyluridine (m3U) by ADAT2/3.
  • Co-expression of TRM140 and ADAT2/3 suppresses the mutagenicity of ADAT2/3, maintaining genome stability.

Conclusions:

  • A model of modification interdependence is demonstrated, where methylation precedes deamination.
  • This sequential modification pathway explains the lack of wholesale deamination in T. brucei.
  • Findings provide insights into the regulation of mutagenic deaminases, including human AID.