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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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Related Experiment Video

Updated: May 31, 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

Precision Chemistry for Protein Lysine Modification.

Mayu Onoda1, Motomu Kanai1

  • 1Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|May 30, 2026
PubMed
Summary

Studying lysine post-translational modifications (PTMs) is vital for understanding cellular signaling. New ligand-guided catalysis offers precise, programmable control over lysine modification, advancing synthetic epigenetics research.

Keywords:
catalysisepigeneticslysinepost‐translational modificationsregioselectivity

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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

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Related Experiment Videos

Last Updated: May 31, 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

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Molecular Biology

Background:

  • Lysine post-translational modifications (PTMs) are critical regulators of protein function, structure, and cellular signaling pathways.
  • Studying PTMs requires homogeneous proteins with site-specific modifications, which is challenging due to the similar chemistry and variable reactivity of lysine residues.
  • Existing chemical methods for lysine modification are often limited in scope and selectivity, especially for less accessible sites.

Purpose of the Study:

  • To develop advanced chemical strategies for achieving regioselective and catalytic modification of lysine residues.
  • To create a platform for the precise installation of authentic PTMs on proteins.
  • To enable programmable control over lysine modification for applications in synthetic epigenetics.

Main Methods:

  • Exploiting enzymatic principles of substrate recognition and spatial organization to guide chemical reactions.
  • Developing ligand-directed chemistry and proximity-enabled modification strategies.
  • Utilizing on-demand generation of highly reactive electrophiles for targeted modifications.
  • Advancing ligand-guided catalysis for selective lysine modification.

Main Results:

  • Demonstrated regioselective and catalytic installation of biorelevant, authentic PTMs.
  • Developed a versatile platform for programmable lysine modification.
  • Overcame limitations of earlier chemical strategies for modifying sterically hindered or low-reactivity lysine sites.

Conclusions:

  • Ligand-guided catalysis represents a significant advancement in achieving precise control over lysine PTMs.
  • This approach provides a powerful tool for synthetic epigenetics and detailed functional studies of PTMs.
  • The developed platform facilitates the generation of homogeneous, site-specifically modified proteins for various biological investigations.