Abstract:
:Histone acetyltransferases (HATs) and histone deacetylases (HDACs) conduct many critical functions through nonhistone substrates in metazoans, but only chromatin-associated nonhistone substrates are known in Saccharomyces cerevisiae. Using yeast proteome microarrays, we identified and validated many nonchromatin substrates of the essential nucleosome acetyltransferase of H4 (NuA4) complex. Among these, acetylation sites (Lys19 and 514) of phosphoenolpyruvate carboxykinase (Pck1p) were determined by tandem mass spectrometry. Acetylation at Lys514 was crucial for enzymatic activity and the ability of yeast cells to grow on nonfermentable carbon sources. Furthermore, Sir2p deacetylated Pck1p both in vitro and in vivo. Loss of Pck1p activity blocked the extension of yeast chronological life span caused by water starvation. In human hepatocellular carcinoma (HepG2) cells, human Pck1 acetylation and glucose production were dependent on TIP60, the human homolog of ESA1. Our findings demonstrate a regulatory function for the NuA4 complex in glucose metabolism and life span by acetylating a critical metabolic enzyme.
journal_name
Celljournal_title
Cellauthors
Lin YY,Lu JY,Zhang J,Walter W,Dang W,Wan J,Tao SC,Qian J,Zhao Y,Boeke JD,Berger SL,Zhu Hdoi
10.1016/j.cell.2009.01.033subject
Has Abstractpub_date
2009-03-20 00:00:00pages
1073-84issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(09)00081-6journal_volume
136pub_type
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