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Related Concept Videos

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: May 14, 2026

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

Using functional proteome microarrays to study protein lysine acetylation.

Jin-Ying Lu1, Yu-Yi Lin, Jef D Boeke

  • 1Department of Laboratory Medicine, National Taiwan University Hospital, Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei, Taiwan.

Methods in Molecular Biology (Clifton, N.J.)
|February 6, 2013
PubMed
Summary

Yeast proteome microarrays identified protein acetylation substrates linked to the essential NuA4 enzyme. This acetylation of metabolic enzymes controls yeast lifespan, impacting aging and longevity pathways.

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Related Experiment Videos

Last Updated: May 14, 2026

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

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

Published on: December 9, 2017

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

Area of Science:

  • Proteomics
  • Biochemistry
  • Molecular Biology

Background:

  • Proteome microarrays offer a high-throughput platform for global biological function exploration.
  • These arrays enable profiling of various protein posttranslational modifications, such as acetylation.

Purpose of the Study:

  • To connect protein lysine acetylation substrates with their upstream modifying enzyme, NuA4, in yeast.
  • To investigate the role of reversible acetylation in regulating cell metabolism and lifespan.

Main Methods:

  • Fabrication and utilization of yeast proteome microarrays.
  • High-throughput screening to identify acetylation substrates and modifying enzymes.

Main Results:

  • Successfully linked protein lysine acetylation substrates to the essential yeast enzyme, nucleosome acetyltransferase of H4 (NuA4).
  • Demonstrated that reversible acetylation of key metabolic enzymes regulates lifespan in yeast.

Conclusions:

  • The study provides a functional dissection of NuA4, a crucial acetylation enzyme.
  • Findings reveal acetylation's role in controlling aging and longevity pathways, offering a paradigm shift in understanding these processes.