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.
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Acknowledgments
The work was supported by National Science Council (NSC 98-2314-B-002-031-MY3 to J.-Y.L.), National Taiwan University Hospital (099-001376 to J.-Y.L.), National Taiwan University (99C101-603 to J.-Y.L. and Y.-Y.L.), Liver Disease Prevention & Treatment Research Foundation (J.-Y.L. and Y.-Y.L.), Taiwan, and the NIH Common Fund Grant (U54-RR020839 to H.Z. and J.D.B.), USA.
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Lu, Jy., Lin, Yy., Boeke, J.D., Zhu, H. (2013). Using Functional Proteome Microarrays to Study Protein Lysine Acetylation. In: Hake, S., Janzen, C. (eds) Protein Acetylation. Methods in Molecular Biology, vol 981. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-305-3_12
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DOI: https://doi.org/10.1007/978-1-62703-305-3_12
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