title: Using functional proteome microarrays to study protein lysine acetylation.
abstract: 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.
authors: Department of Laboratory Medicine, National Taiwan University Hospital, Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei, Taiwan.
authors: Jin-Ying
authors: JY
authors: Lu
authors: Yu-Yi
authors: YY
authors: Lin
authors: Jef D
authors: JD
authors: Boeke
authors: Heng
authors: H
authors: Zhu
mesh_terms: D000107:Acetylation; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D051548:Histone Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry / Q000378:metabolism*; D040081:Protein Array Analysis / Q000379:methods*; D011499:Protein Processing, Post-Translational; D020543:Proteome; D015003:Yeasts / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D020543:Proteome; D051548:Histone Acetyltransferases; D008239:Lysine