4.6 Article

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

期刊

JOURNAL OF BIOLOGICAL CHEMISTRY
卷 294, 期 7, 页码 2279-2292

出版社

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.RA118.006914

关键词

isotope effect; cell growth; hydrogen-deuterium exchange; protein stability; enzyme kinetics; proteomics; clusters of orthologous groups database; deuteration; gene ontology database; isotope labeling; kinetic isotope effect; biomolecular stability; minimal medium

资金

  1. Swiss National Science Foundation [31-149927, 31-173089]

向作者/读者索取更多资源

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.

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