In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate

Chi Ho Chan, Jane Garrity, Heidi A. Crosby, Jorge C. Escalante-Semerena

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

Acetyl-coenzyme A synthetase (Acs) activates acetate into acetyl-coenzyme A (Ac-CoA) in most cells. In Salmonella enterica, acs expression and Acs activity are controlled. It is unclear why the sirtuin-dependent protein acylation/deacylation system (SDPADS) controls the activity of Acs. Here we show that, during growth on 10mM acetate, acs+ induction in a S. enterica strain that cannot acetylate (i.e. inactivate) Acs leads to growth arrest, a condition that correlates with a drop in energy charge (0.17) in the acetylation-deficient strain, relative to the energy charge in the acetylation-proficient strain (0.71). Growth arrest was caused by elevated Acs activity, a conclusion supported by the isolation of a single-amino-acid variant (AcsG266S), whose overproduction did not arrest growth. Acs-dependent depletion of ATP, coupled with the rise in AMP levels, prevented the synthesis of ADP needed to replenish the pool of ATP. Consistent with this idea, overproduction of ADP-forming Ac-CoA-synthesizing systems did not affect the growth behaviour of acetylation-deficient or acetylation-proficient strains. The AcsG266S variant was >2 orders of magnitude less efficient than the AcsWT enzyme, but still supported growth on 10mM acetate. This work provides the first evidence that SDPADS function helps cells maintain energy homeostasis during growth on acetate.

Original languageEnglish (US)
Pages (from-to)168-183
Number of pages16
JournalMolecular Microbiology
Volume80
Issue number1
DOIs
StatePublished - Apr 2011

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