期刊
BIOCHEMICAL JOURNAL
卷 443, 期 -, 页码 655-661出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20120118
关键词
general control of amino acid synthesis 5 (GCN5)-like 1 (GCN5L1); mitochonclrial metabolism; protein acetylation; sirtuin 3 (SIRT3)
资金
- Division of Intramural Research of the NHLBI (National Heart, Lung and Blood Institute), NIH (National Institutes of Health)
SIRT3 (sirtuin 3) modulates respiration via the deacetylation of lysine residues in electron transport chain proteins. Whether mitochondria] protein acetylation is controlled by a counter-regulatory program has remained elusive. In the present study we identify an essential component of this previously undefined mitochondrial acetyltransferase system. We show that GCN5L1 [GCN5 (general control of amino acid synthesis 5)-like 1; also known as Bloc l s1] counters the acetylation and respiratory effects of SIRT3. GCN5L1 is mitochondrial-enriched and displays significant homology with a prokaryotic acetyltransferase. Genetic knockdown of GCN5L1 blunts mitochondrial protein acetylation, and its reconstitution in intact mitochondria restores protein acetylation. GCN5L1 interacts with and promotes acetylation of SIRT3 respiratory chain targets and reverses global SIRT3 effects on mitochondrial protein acetylation, respiration and bioenergetics. The results of the present study identify GCN5L1 as a critical prokaryote-derived component of the mitochondria] acetyltransferase programme.
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