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Phase II Reactions: Methylation Reactions01:17

Phase II Reactions: Methylation Reactions

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Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
The mechanism of methylation unfolds in two stages. The first stage sees a methyltransferase enzyme facilitating the transfer of a methyl group from S-adenosylmethionine (SAM) to the substrate, forming S-adenosylhomocysteine (SAH). The second stage involves further metabolism of SAH into homocysteine, which can be recycled...
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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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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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.
Writers
The writer...
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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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Related Experiment Video

Updated: Sep 29, 2025

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

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Special Issue "Structure, Activity, and Function of Protein Methyltransferases".

Arunkumar Dhayalan1, Albert Jeltsch2

  • 1Department of Biotechnology, Pondicherry University, Puducherry 605014, India.

Life (Basel, Switzerland)
|March 25, 2022
PubMed
Summary

Post-translational modifications (PTMs) greatly increase protein functional diversity. Understanding PTMs is crucial for deciphering complex biological processes and disease mechanisms.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Proteomics
  • Cellular Signaling

Background:

  • Proteins undergo post-translational modifications (PTMs) after synthesis, significantly expanding their functional repertoire beyond the genetic code.
  • PTMs regulate nearly all aspects of cellular life, including protein stability, localization, interactions, and enzymatic activity.
  • Aberrant PTMs are implicated in numerous human diseases, highlighting their critical roles in health and pathology.

Discussion:

  • The study explores the diverse landscape of PTMs and their impact on proteome complexity.
  • Investigating PTMs provides insights into cellular regulatory networks and signaling pathways.
  • Understanding the interplay of different PTMs is essential for a comprehensive view of protein function.

Key Insights:

  • Post-translational modifications (PTMs) are fundamental to expanding proteome functional diversity.
  • PTMs regulate critical cellular functions and are key players in biological signaling.
  • The combinatorial nature of PTMs creates a complex regulatory network.

Outlook:

  • Future research will focus on the dynamic interplay of PTMs and their roles in disease.
  • Developing novel tools for PTM detection and analysis will advance proteomic studies.
  • Elucidating PTM networks will pave the way for targeted therapeutic strategies.