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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.
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Histone Modification02:32

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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.
Acetylation
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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.
X-chromosome...
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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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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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Related Experiment Video

Updated: Mar 2, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
08:48

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

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Proteins with Site-Specific Lysine Methylation.

Zhipeng A Wang1, Wenshe R Liu1

  • 1Chemistry Department, Texas A&M University, College Station, TX, 77843, USA.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|May 14, 2017
PubMed
Summary

Lysine methylation, an epigenetic mark, regulates proteins distinctly at mono-, di-, and trimethylation levels. Chemical biology methods aid in characterizing these marks for epigenetic studies.

Keywords:
chromatinhistonelysine dimethylationlysine monomethylationposttranslational lysine methylation

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Area of Science:

  • Biochemistry
  • Epigenetics
  • Chemical Biology

Background:

  • Lysine methylation is a crucial epigenetic modification.
  • It regulates both chromatin and non-chromatin proteins.
  • Distinct biological roles exist for mono-, di-, and trimethylation states.

Purpose of the Study:

  • To highlight chemical biology methods for lysine methylation characterization.
  • To discuss applications in epigenetic research.
  • To provide a conceptual overview of developments.

Main Methods:

  • Review of chemical biology techniques.
  • Discussion of biochemical characterization strategies.
  • Focus on methods applicable to epigenetic investigations.

Main Results:

  • Multiple chemical biology methods have been developed.
  • These methods enable the biochemical characterization of lysine methylation.
  • Applications in understanding protein function are demonstrated.

Conclusions:

  • Chemical biology offers powerful tools for studying lysine methylation.
  • These methods are vital for advancing epigenetic research.
  • Understanding lysine methylation is key to protein function regulation.