Label-free MS/MS analyses of the dinoflagellate Lingulodinium identifies rhythmic proteins facilitating adaptation to a diurnal LD cycle
| Autor: | Samuel Chun-Lap Lo, David Morse, Sirius P.K. Tse, Carl Bowazolo, Mathieu Beauchemin, Jean Rivoal |
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| Rok vydání: | 2019 |
| Předmět: |
Proteomics
Environmental Engineering 010504 meteorology & atmospheric sciences Proteome Acclimatization 010501 environmental sciences 01 natural sciences Aconitase Tandem Mass Spectrometry Environmental Chemistry Luciferase Photosynthesis Waste Management and Disposal 0105 earth and related environmental sciences chemistry.chemical_classification biology Dinoflagellate biology.organism_classification Pollution Amino acid Enzyme Biochemistry chemistry Dinoflagellida Lingulodinium polyedrum Flux (metabolism) Chromatography Liquid |
| Zdroj: | The Science of the total environment. 704 |
| ISSN: | 1879-1026 |
| Popis: | Protein levels were assessed in the dinoflagellate Lingulodinium polyedra over the course of a diurnal cycle using a label-free LC-MS/MS approach. Roughly 1700 proteins were quantitated in a triplicate dataset over a daily period, and 13 were found to show significant rhythmic changes. Included among the proteins found to be most abundant at night were the two bioluminescence proteins, luciferase and luciferin binding protein, as well as a proliferating cell nuclear protein involved in the nightly DNA replication. Aconitase and a pyrophosphate fructose-6-phosphate-1-phosphotransferase were also found to be more abundant at night, suggestive of an increased ability to generate ATP by glucose catabolism when photosynthesis does not occur. Among the proteins more abundant during the day were found a 2-epi-5-epi-valiolone synthase, potentially involved in synthesis of mycosporin-like amino acids that can act as a “microbial sunscreen”, and an enzyme synthesizing vitamin B6 which is known to protect against oxidative stress. A lactate oxidoreductase was also found to be more abundant during the day, perhaps to counteract the pH changes due to carbon fixation by facilitating conversion of pyruvate to lactate. This unbiased proteomic approach reveals novel insights into the daily metabolic changes of this dinoflagellate. Furthermore, the observation that only a limited number of proteins vary support a model where metabolic flux through pathways can be controlled by variations in a select few, possibly rate limiting, steps. Data are available via ProteomeXchange with identifier PXD006994. |
| Databáze: | OpenAIRE |
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