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Relative impact of three growth conditions on the Escherichia coli protein acetylome

dc.contributor.authorLozano- Terol, Gema
dc.contributor.authorZenezini Chiozzi, Riccardo
dc.contributor.authorSola-Martínez, Rosa Alba
dc.contributor.authorHeck, Albert J.R.
dc.contributor.authorCánovas Díaz, Manuel
dc.contributor.authorDiego Puente, Teresa de
dc.contributor.authorGallego Jara, Julia
dc.contributor.authorMartínez Vivancos, Adrián
dc.contributor.authorOrtega Retuerta, Álvaro
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2024-12-13T12:31:09Z
dc.date.available2024-12-13T12:31:09Z
dc.date.issued2024-02-16
dc.description© 2024 Elsevier. This document is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0 This document is the publishec version of a published work that appeared in final form in IScience To access the final work, see DOI: https://doi.org/10.1016/j.isci.2024.109017
dc.description.abstractNε-lysine acetylation is a common posttranslational modification observed in Escherichia coli. In the present study, integrative analysis of the proteome and acetylome was performed using label-free quantitative mass spectrometry to analyze the relative influence of three factors affecting growth. The results revealed differences in the proteome, mainly owing to the type of culture medium used (defined or complex). In the acetylome, 7482 unique acetylation sites were identified. Acetylation is directly related to the abundance of proteins, and the level of acetylation in each type of culture is associated with extracellular acetate concentration. Furthermore, most acetylated lysines in the exponential phase remained in the stationary phase without dynamic turnover. Interestingly, unique acetylation sites were detected in proteins whose presence or abundance was linked to the type of culture medium. Finally, the biological function of the acetylation changes was demonstrated for three central metabolic proteins (GapA, Mdh, and AceA).es
dc.formatapplication/pdfes
dc.format.extent20es
dc.identifier.citationiScience 27, 109017, February 16, 2024 109017
dc.identifier.doihttps://doi.org/10.1016/ j.isci.2024.109017
dc.identifier.urihttp://hdl.handle.net/10201/147441
dc.languageenges
dc.publisherCell Presses
dc.relationThis work has been supported by EPIC-XS, project number 823839, funded by the Horizon 2020 programme of the European Union. This work has also been financed by the project PID2021-122202OB-I00 funded by MCIN/AEI/10.13039/501100011033 and by ‘‘ERDF A way of making Europe’’, by the ‘‘European Union’’. G.L.-T. is recipient of a PhD fellowship from (20715/FPI/18) Fundación Séneca. Region of Murcia (Spain), R.A.S.-M. is recipient of a grant ‘‘Margarita Salas’’ from University of Murcia (133/MSJD/22), financed by the Ministry of Universities, by the European Union – NextGenerationEU and the Recovery, Transformation and Resilience Plan, and A.M.V. is recipient of an FPU-PhD fellowship from the University of Murcia.es
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S2589004224002384?via%3Dihub
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectProtein acetylome,es
dc.subjectEscherichia coli
dc.subjectNε-lysine acetylation
dc.subject.otherCDU::6 - Ciencias aplicadases
dc.titleRelative impact of three growth conditions on the Escherichia coli protein acetylomees
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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relation.isAuthorOfPublication.latestForDiscovery57bf3537-1124-49ab-8774-bd0c3bdf1c28
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