Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 진언선 | - |
dc.date.accessioned | 2022-12-05T04:10:16Z | - |
dc.date.available | 2022-12-05T04:10:16Z | - |
dc.date.issued | 2022-03 | - |
dc.identifier.citation | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v. 23, NO. 5, article no. 2710, Page. 1-18 | en_US |
dc.identifier.issn | 1661-6596;1422-0067 | en_US |
dc.identifier.uri | https://www.mdpi.com/1422-0067/23/5/2710 | en_US |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/177913 | - |
dc.description.abstract | The chloroplast protein CP12 is involved in the dark/light regulation of the Calvin-Benson-Bassham cycle, in particular, in the dark inhibition of two enzymes: glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK), but other functions related to stress have been proposed. We knocked out the unique CP12 gene to prevent its expression in Chlamydomonas reinhardtii (Delta CP12). The growth rates of both wild-type and Delta CP12 cells were nearly identical, as was the GAPDH protein abundance and activity in both cell lines. On the contrary, the abundance of PRK and its specific activity were significantly reduced in Delta CP12, as revealed by relative quantitative proteomics. Isolated PRK lost irreversibly its activity over-time in vitro, which was prevented in the presence of recombinant CP12 in a redox-independent manner. We have identified amino acid residues in the CP12 protein that are required for this new function preserving PRK activity. Numerous proteins involved in redox homeostasis and stress responses were more abundant and the expressions of various metabolic pathways were also increased or decreased in the absence of CP12. These results highlight CP12 as a moonlighting protein with additional functions beyond its well-known regulatory role in carbon metabolism. | en_US |
dc.description.sponsorship | C.G.’s studentship (ED62) is supported by the Ministère de la Recherche, de l’Enseignement supérieur et de l’Innovation. E.L. studentship was supported by IM2 B—AMIDEX fellowship AAP-IM2 B-NE−2020–02-Launay. BG, HL, FC: this research was supported by the Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université. HL: HL acknowledges the FEBS for the research grant Launay Excellence Award, 2021. ES. J.: This research was funded by the Basic Science Research Program (NRF−2020 R1 A2 C2011998) and the “Carbon to X Project” (2020 M3 H7 A1098294) of the National Research Foundation (NRF) of Korea. Marseille Protéomique (MaP) is a proteomic platform IBiSA- and Aix-Marseille Université labelled. | en_US |
dc.language | en | en_US |
dc.publisher | MDPI | en_US |
dc.source | 84341_진언선.pdf | - |
dc.subject | Calvin-Benson-Bassham | en_US |
dc.subject | CP12 | en_US |
dc.subject | enzymatic activity | en_US |
dc.subject | intrinsically disordered protein | en_US |
dc.subject | quantitative proteomics | en_US |
dc.subject | photosynthesis | en_US |
dc.subject | glyoxylate pathway | en_US |
dc.subject | carbon allocation | en_US |
dc.subject | nitrogen uptake | en_US |
dc.title | Reduction in Phosphoribulokinase Amount and Re-Routing Metabolism in Chlamydomonas reinhardtii CP12 Mutants | en_US |
dc.type | Article | en_US |
dc.relation.no | 5 | - |
dc.relation.volume | 23 | - |
dc.identifier.doi | 10.3390/ijms23052710 | en_US |
dc.relation.page | 1-18 | - |
dc.relation.journal | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | - |
dc.contributor.googleauthor | Gerard, Cassy | - |
dc.contributor.googleauthor | Lebrun, Regine | - |
dc.contributor.googleauthor | Lemesle, Erwan | - |
dc.contributor.googleauthor | Avilan, Luisana | - |
dc.contributor.googleauthor | Chang, Kwang Suk | - |
dc.contributor.googleauthor | Jin, EonSeon | - |
dc.contributor.googleauthor | Carriere, Frederic | - |
dc.contributor.googleauthor | Gontero, Brigitte | - |
dc.contributor.googleauthor | Launay, Helene | - |
dc.sector.campus | S | - |
dc.sector.daehak | 자연과학대학 | - |
dc.sector.department | 생명과학과 | - |
dc.identifier.pid | esjin | - |
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