Publication: Relative impact of three growth conditions on the Escherichia coli protein acetylome
Authors
Lozano- Terol, Gema ; Zenezini Chiozzi, Riccardo ; Sola-Martínez, Rosa Alba ; Heck, Albert J.R. ; Cánovas Díaz, Manuel ; Diego Puente, Teresa de ; Gallego Jara, Julia ; Martínez Vivancos, Adrián ; Ortega Retuerta, Álvaro
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Publisher
Cell Press
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DOI
https://doi.org/10.1016/ j.isci.2024.109017
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info:eu-repo/semantics/article
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
Abstract
Nε-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).
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Citation
iScience 27, 109017, February 16, 2024 109017
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