Using functional proteome microarrays to study protein lysine acetylation

Jin Ying Lu, Yu Yi Lin, Jef D. Boeke, Heng Zhu

Research output: Chapter in Book/Report/Conference proceedingChapter


Emergence of proteome microarray provides a versatile platform to globally explore biological functions of broad significance. In the past decade, researchers have successfully fabricated functional proteome microarrays by printing individually purified proteins at a high-throughput, proteome-wide scale on one single slide. These arrays have been used to profile protein posttranslational modifications, including phosphorylation, ubiquitylation, acetylation, and nitrosylation. In this chapter, we summarize our work of using the yeast proteome microarrays to connect protein lysine acetylation substrates to their upstream modifying enzyme, the nucleosome acetyltransferase of H4 (NuA4), which is the only essential acetyltransferase in yeast. We further prove that the reversible acetylation on critical cell metabolism-related enzymes controls life span in yeast. Our studies represent a paradigm shift for the functional dissection of a crucial acetylation enzyme affecting aging and longevity pathways.

Original languageEnglish (US)
Title of host publicationProtein Acetylation
Subtitle of host publicationMethods and Protocols
PublisherHumana Press Inc.
Number of pages15
ISBN (Print)9781627033046
StatePublished - 2013

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Aging
  • Functional proteome microarray
  • Longevity
  • Lysine acetylation
  • Posttranslational modification
  • Protein chip

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


Dive into the research topics of 'Using functional proteome microarrays to study protein lysine acetylation'. Together they form a unique fingerprint.

Cite this