Dataset Information

Elucidating the diverse roles of acetyl-CoA in the cytosol and mitochondrion of Toxoplasma gondii

ABSTRACT: Acetyl-CoA is a key metabolite in all organisms, implicated in transcriptional regulation, post-translational modification as well as fuelling the TCA cycle and the synthesis and elongation of fatty acids. The obligate intracellular parasite Toxoplasma gondii possesses two enzymes which produce acetyl-CoA in the cytosol and nucleus: the acetyl-CoA synthase (ACS) and the ATP-citrate lyase (ACL), while the branched chain α-ketoacid dehydrogenase (BCKDH) generates acetyl-CoA in the mitochondrion. Given the diverse functions of acetyl-CoA, we know little about the specific roles of distinct sub-cellular acetyl-CoA pools and how these impact overall parasite physiology. To assess the broad functions of nucleo-cytosolic as well as mitochondrial acetyl-CoA, we analysed the acetylome and total proteome of parasites lacking ACL/ACS or BCKDH.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Toxoplasma Gondii Rh

SUBMITTER: Yohann Couté

LAB HEAD: Virginie Brun

PROVIDER: PXD016133 | Pride | 2020-05-07

REPOSITORIES: Pride

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Multi-omics analysis delineates the distinct functions of sub-cellular acetyl-CoA pools in Toxoplasma gondii.

Kloehn Joachim J Oppenheim Rebecca D RD Siddiqui Ghizal G De Bock Pieter-Jan PJ Kumar Dogga Sunil S Coute Yohann Y Hakimi Mohamed-Ali MA Creek Darren J DJ Soldati-Favre Dominique D

BMC biology 20200616 1

<h4>Background</h4>Acetyl-CoA is a key molecule in all organisms, implicated in several metabolic pathways as well as in transcriptional regulation and post-translational modification. The human pathogen Toxoplasma gondii possesses at least four enzymes which generate acetyl-CoA in the nucleo-cytosol (acetyl-CoA synthetase (ACS); ATP citrate lyase (ACL)), mitochondrion (branched-chain α-keto acid dehydrogenase-complex (BCKDH)) and apicoplast (pyruvate dehydrogenase complex (PDH)). Given the dive ...[more]

PMID: 32546260

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Project description:The strictly anaerobic bacterium Dehalococcoides mccartyi is obligatory dependent on organohalide respiration for energy conservation and growth. Due to its capability to reductively dehalogenate a multitude of toxic halogenated electron acceptors, it plays an important role in the attenuation of these compounds at respective contaminated sites. Here, D. mccartyi strain CBDB1, specialized on the dehalogenation of chloroaromatic compounds, was grown in a two-liquid phase system with 1,2,3-trichlorobenzene as electron acceptor, acetate plus CO2 as carbon source and hydrogen as electron donor. The proteome and Nε-lysine acetylome were analyzed in the lag, exponential and stationary phases. The high and almost invariable abundance of the membrane-localized organohalide respiration complex consisting of the reductive dehalogenases CbrA and CbdbA80, the uptake hydrogenase HupLS and the organohalide respiration molybdoenzyme OmeAB was shown throughout growth and also after a prolonged stationary phase. Quantification of transcripts of reductive dehalogenase genes revealed their major synthesis starting in the lag phase, which might be a prerequisite for balanced growth in the exponential phase. The analyses of the coverage of functional pathways as well as indicator analysis revealed the growth-phase specificity of the proteome, with regulatory proteins identified as important indicators for the stationary phase. The number of acetylated proteins increased from the lag to the stationary phase. We detected pronounced acetylation of key proteins of the acetate metabolism, i.e. the synthesis of acetyl-CoA and its processing via gluconeogenesis and the incomplete Wood-Ljungdahl pathway, as well as of proteins central for the biosynthesis of amino acids, co-factors and terpenoids. In addition, the partial acetylation of the reductive dehalogenases as well as of TatA, a component of the twin-arginine translocation machinery, suggests that acetylation might be directly involved in the maintenance of the organohalide respiration capacity of D. mccartyi over periods without access to halogenated electron acceptors.

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