Proteomics

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Dictyostelium DIA LFQ proteomics of vegetative and developmental growth


ABSTRACT: Dictyostelium discoideum behavior depends on nutrients. When sufficient food is present these amoebae exist in a unicellular state (vegetative growth), but upon starvation they aggregate into a multicellular organism (developmental growth). For proteomics 30 minutes and eight hour cultures of D. discoideum under vegetative and starved growth conditions were compared by DIA-LFQ. This unique biology makes D. discoideum an ideal model for investigating how fundamental metabolism commands cell differentiation and function. We show here that reactive oxygen species (ROS), generated as a consequence of nutrient limitation, lead to the sequestration of the amino acid cysteine in the antioxidant glutathione, limiting the use of its sulfur atom for processes such as protein translation and FeS cluster-containing enzyme activity that contribute to mitochondrial metabolism and cellular proliferation. Such regulated sulfur sequestration maintains D. discoideum in a non-proliferating state that paves the way for multicellular development. This new mechanism of ROS signaling highlights oxygen and sulfur as simple, early evolutionary signaling molecules dictating cell fate, with implications for responses to nutrient fluctuations in higher eukaryotes.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Dictyostelium Discoideum (slime Mold)

SUBMITTER: Gerhard Mittler  

LAB HEAD: Gerhard Mittler

PROVIDER: PXD023404 | Pride | 2021-03-23

REPOSITORIES: Pride

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The behaviour of Dictyostelium discoideum depends on nutrients<sup>1</sup>. When sufficient food is present these amoebae exist in a unicellular state, but upon starvation they aggregate into a multicellular organism<sup>2,3</sup>. This biology makes D. discoideum an ideal model for investigating how fundamental metabolism commands cell differentiation and function. Here we show that reactive oxygen species-generated as a consequence of nutrient limitation-lead to the sequestration of cysteine i  ...[more]

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