{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zheng L"],"funding":["Wellcome Trust"],"pagination":["2557"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11910552"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Acetyl-CoA synthetase (Acs) generates acetyl-coenzyme A (Ac-CoA) but its excessive activity can deplete ATP and lead to a growth arrest. To prevent this, Acs is regulated through Ac-CoA-dependent feedback inhibition executed by Ac-CoA-dependent acetyltransferases such as AcuA in Bacillus subtilis. AcuA acetylates the catalytic lysine of AcsA turning the synthetase inactive. Here, we report that AcuA and AcsA form a tightly intertwined complex - the C-terminal domain binds to acetyltransferase domain of AcuA, while the C-terminus of AcuA occupies the CoA-binding site in the N-terminal domain of AcsA. Formation of the complex reduces AcsA activity in addition to the well-established acetylation of the catalytic lysine 549 in AcsA which we show can disrupt the complex. Thus, different modes o"],"journal":["Nature communications"],"pubmed_title":["Regulation of acetyl-CoA biosynthesis via an intertwined acetyl-CoA synthetase/acetyltransferase complex."],"pmcid":["PMC11910552"],"funding_grant_id":["WT096570"],"pubmed_authors":["Steinchen W","Bedrunka P","Bekeredjian-Ding I","Zheng L","Abendroth F","Du Y","Freitag J","Bange G","Jalomo-Khayrova E","Girbig M","Hochberg GKA","Mais CN"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of acetyl-CoA biosynthesis via an intertwined acetyl-CoA synthetase/acetyltransferase complex.","description":"Acetyl-CoA synthetase (Acs) generates acetyl-coenzyme A (Ac-CoA) but its excessive activity can deplete ATP and lead to a growth arrest. To prevent this, Acs is regulated through Ac-CoA-dependent feedback inhibition executed by Ac-CoA-dependent acetyltransferases such as AcuA in Bacillus subtilis. AcuA acetylates the catalytic lysine of AcsA turning the synthetase inactive. Here, we report that AcuA and AcsA form a tightly intertwined complex - the C-terminal domain binds to acetyltransferase domain of AcuA, while the C-terminus of AcuA occupies the CoA-binding site in the N-terminal domain of AcsA. Formation of the complex reduces AcsA activity in addition to the well-established acetylation of the catalytic lysine 549 in AcsA which we show can disrupt the complex. Thus, different modes o","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-06-02T21:08:58.903Z","creation":"2025-04-20T00:10:21.119Z"},"accession":"S-EPMC11910552","cross_references":{"pubmed":["40089509"],"doi":["10.1038/s41467-025-57842-2"]}}