Deuterium induces a distinctive; Escherichia coli; proteome that correlates with the reduction in growth rate

Opitz, Christian and Ahrné, Erik and Goldie, Kenneth N. and Schmidt, Alexander and Grzesiek, Stephan. (2019) Deuterium induces a distinctive; Escherichia coli; proteome that correlates with the reduction in growth rate. Journal of Biological Chemistry, 294 (7). pp. 2279-2292.

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Official URL: https://edoc.unibas.ch/78557/

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Substitution of protium (H) for deuterium (D) strongly affects biological systems. Whereas higher eukaryotes such as plants and mammals hardly survive a deuterium content of >30%, many microorganisms can grow on fully deuterated media, albeit at reduced rates. Very little is known about how the H/D replacement influences life at the systems level. Here, we used MS-based analysis to follow the adaptation of a large part of the; Escherichia coli; proteome from growth on a protonated full medium, over a protonated minimal medium, to a completely deuterated minimal medium. We could quantify >1800 proteins under all conditions, several 100 of which exhibited strong regulation during both adaptation processes. The adaptation to minimal medium strongly up-regulated amino acid synthesis and sugar metabolism and down-regulated translational proteins on average by 9%, concomitant with a reduction in growth rate from 1.8 to 0.67 h; -1; In contrast, deuteration caused a very wide proteomic response over many cell functional categories, together with an additional down-regulation of the translational proteins by 5%. The latter coincided with a further reduction in growth rate to 0.37 h; -1; , revealing a clear linear correlation between growth rate and abundance of translational proteins. No significant morphological effects are observed under light and electron microscopies. Across all protein categories, about 80% of the proteins up-regulated under deuteration are enzymes with hydrogen transfer functions. Thus, the H/D kinetic isotope effect appears as the major limiting factor of cellular functions under deuteration.
Faculties and Departments:05 Faculty of Science
UniBasel Contributors:Goldie, Kenneth N.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Biochemistry and Molecular Biology
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:01 Oct 2020 07:22
Deposited On:01 Oct 2020 07:22

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