LUPETTE, Josselin; TARDIF, Marianne; BRUGIERE, Sabine; COUTE, Yohann; SALVAING, Juliette; MARECHAL, Eric

doi:10.1002/pmic.202200155

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LUPETTE, Josselin
Laboratoire de biogenèse membranaire [LBM]

TARDIF, Marianne

BRUGIERE, Sabine

Langue

Article de revue

Ce document a été publié dans

Proteomics. 2022, vol. 22, n° 22, p. 2200155

Résumé en anglais

Diatoms are one of the largest groups in phytoplankton biodiversity. Understanding their response to nitrogen variations, present from micromolar to near-zero levels in oceans and fresh waters, is essential to comprehend their ecological success. Nitrogen starvation is used in biotechnological processes, to trigger the remodeling of carbon metabolism in the direction of fatty acids and triacylglycerol synthesis. We evaluated whole proteome changes in Phaeodactylum tricornutum after 7 days of cultivation with 5.5-mM nitrate (+N) or without any nitrogen source (-N). On a total of 3768 proteins detected in biological replicates, our analysis pointed to 384 differentially abundant proteins (DAP). Analysis of proteins of lower abundance in -N revealed an arrest of amino acid and protein syntheses, a remodeling of nitrogen metabolism, and a decrease of the proteasome abundance suggesting a decline in unselective whole-proteome decay. Analysis of proteins of higher abundance revealed the setting up of a general nitrogen scavenging system dependent on deaminases. The increase of a plastid palmitoyl-ACP desaturase appeared as a hallmark of carbon metabolism rewiring in the direction of fatty acid and triacylglycerol synthesis. This dataset is also valuable to select gene candidates for improved biotechnological properties.< Réduire

Mots clés en anglais

Diatom

Nitrogen starvation

Phaeodactylum

Proteome remodelling

Quantitative proteomics

URI

https://oskar-bordeaux.fr/handle/20.500.12278/171802

DOI

http://dx.doi.org/10.1002/pmic.202200155

Project ANR

CBH-EUR-GS - ANR-17-EURE-0003
Grenoble Alliance for Integrated Structural Cell Biology - ANR-10-LABX-0049
Infrastructure Française de Protéomique - ANR-10-INBS-0008
IDEX UGA - ANR-15-IDEX-0002

Unités de recherche

Laboratoire de Biogenèse Membranaire (LBM) - UMR 5200