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Responses of the marine diatom Thalassiosira pseudonana to changes in CO2 concentration: a proteomic approach

Clement, Romain; Lignon, Sabrina; Mansuelle, Pascal; Jensen, Erik; Pophillat, Matthieu; Lebrun, Regine; Denis, Yann; Puppo, Carine; Maberly, Stephen C. ORCID: https://orcid.org/0000-0003-3541-5903; Gontero, Brigitte. 2017 Responses of the marine diatom Thalassiosira pseudonana to changes in CO2 concentration: a proteomic approach. Scientific Reports, 7, 42333. 12, pp. 10.1038/srep42333

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Abstract/Summary

The concentration of CO2 in many aquatic systems is variable, often lower than the KM of the primary carboxylating enzyme Rubisco, and in order to photosynthesize efficiently, many algae operate a facultative CO2 concentrating mechanism (CCM). Here we measured the responses of a marine diatom, Thalassiosira pseudonana, to high and low concentrations of CO2 at the level of transcripts, proteins and enzyme activity. Low CO2 caused many metabolic pathways to be remodeled. Carbon acquisition enzymes, primarily carbonic anhydrase, stress, degradation and signaling proteins were more abundant while proteins associated with nitrogen metabolism, energy production and chaperones were less abundant. A protein with similarities to the Ca2+/ calmodulin dependent protein kinase II_association domain, having a chloroplast targeting sequence, was only present at low CO2. This protein might be a specific response to CO2 limitation since a previous study showed that other stresses caused its reduction. The protein sequence was found in other marine diatoms and may play an important role in their response to low CO2 concentration.

Item Type: Publication - Article
Digital Object Identifier (DOI): 10.1038/srep42333
UKCEH and CEH Sections/Science Areas: Parr
ISSN: 2045-2322
Additional Information. Not used in RCUK Gateway to Research.: Open Access paper - full text available via Official URL link.
NORA Subject Terms: Marine Sciences
Botany
Date made live: 13 Feb 2017 11:10 +0 (UTC)
URI: https://nora.nerc.ac.uk/id/eprint/516168

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