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Related Concept Videos

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.
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: Jun 4, 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 functional protein microarray approach to characterizing posttranslational modifications on lysine residues.

Jun Seop Jeong1, Hee-Sool Rho, Heng Zhu

  • 1Department of Pharmacology and Molecular Sciences, High Throughput Biology Center, Johns Hopkins School of Medicine, Baltimore, MD, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 4, 2011
PubMed
Summary

Functional protein microarrays enable global identification of enzyme-substrate interactions, particularly for lysine posttranslational modifications (PTMs). This study details protocols for investigating ubiquitylation and acetylation, advancing PTM research across organisms.

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Last Updated: Jun 4, 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

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Posttranslational modifications (PTMs) on lysine residues are crucial regulatory mechanisms in biological processes.
  • Identifying enzyme-substrate interactions for PTMs, such as ubiquitylation and acetylation, is challenging with traditional methods.

Purpose of the Study:

  • To present detailed protocols for investigating ubiquitylation and acetylation using functional protein microarrays.
  • To highlight the utility of protein microarrays for global enzyme-substrate interaction discovery, focusing on lysine PTMs.

Main Methods:

  • Development and application of functional protein microarrays for different model organisms.
  • Utilizing yeast proteome chips to identify substrates of specific enzymes like the ubiquitin E3 ligase Rsp5.
  • Characterizing acetylation events on nonhistone substrates, including metabolic enzymes.

Main Results:

  • Identification of downstream substrates for the ubiquitin E3 ligase Rsp5.
  • Discovery of nonhistone substrates for the acetyltransferase NuA4 complex in yeast.
  • Demonstration that reversible acetylation of a metabolic enzyme impacts glucose metabolism and lifespan.

Conclusions:

  • Functional protein microarrays are powerful tools for dissecting enzyme-substrate interactions and PTMs.
  • The presented protocols offer a broadly applicable methodology for studying ubiquitylation and acetylation in various organisms.
  • This research advances the understanding of lysine PTMs in fundamental biological processes.