Proteomics

Dataset Information

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Characterization of lysine acetylation in Toxoplasma gondii proteome lacking acetyl-CoA transporter 1 (AT1).


ABSTRACT: Acetyl-CoA participates in post-translational modification of proteins, central carbon and lipid metabolism in several cell compartments. In mammals, the acetyl-CoA transporter 1 (AT1) facilitates the flux of cytosolic acetyl-CoA into the endoplasmic reticulum (ER), enabling the acetylation of proteins of the secretory pathway, in concert with dedicated acetyltransferases including Nat8. However, the implication of the ER acetyl-CoA pool in acetylation of ER-transiting proteins and their relevance throughout the parasites’ life cycle is unknown. Here, we evaluated the impact of blocking putative cytosolic acetyl-CoA import on acetylation of proteins through KO of the homologue of AT1 in the parasite Toxoplasma gondii.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human) Toxoplasma Gondii Rh

SUBMITTER: Yohann Couté  

LAB HEAD: Yohann Couté

PROVIDER: PXD030932 | Pride | 2022-07-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
HF1_012540.raw Raw
HF1_012542.raw Raw
HF1_012544.raw Raw
HF1_012546.raw Raw
HF1_012548.raw Raw
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Publications

N-acetylation of secreted proteins in Apicomplexa is widespread and is independent of the ER acetyl-CoA transporter AT1.

Nyonda Mary Akinyi MA   Boyer Jean-Baptiste JB   Belmudes Lucid L   Krishnan Aarti A   Pino Paco P   Couté Yohann Y   Brochet Mathieu M   Meinnel Thierry T   Soldati-Favre Dominique D   Giglione Carmela C  

Journal of cell science 20220805 15


Acetyl-CoA participates in post-translational modification of proteins and in central carbon and lipid metabolism in several cell compartments. In mammals, acetyl-CoA transporter 1 (AT1, also known as SLC33A1) facilitates the flux of cytosolic acetyl-CoA into the endoplasmic reticulum (ER), enabling the acetylation of proteins of the secretory pathway, in concert with the activity of dedicated acetyltransferases such as NAT8. However, the involvement of the ER acetyl-CoA pool in acetylation of E  ...[more]

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