Proteomic dissection of the chloroplast: Moving beyond photosynthesis

dc.contributor.authorLande, Nilesh Vikram
dc.contributor.authorBarua, Pragya
dc.contributor.authorGayen, Dipak
dc.contributor.authorKumar, Sunil
dc.contributor.authorChakraborty, Subhra
dc.contributor.authorChakraborty, Niranjan
dc.date.accessioned2019-11-14T11:02:58Z
dc.date.available2019-11-14T11:02:58Z
dc.date.issued2020
dc.descriptionAccepted date: 5 November 2019en_US
dc.description.abstractChloroplast, the photosynthetic machinery, converts photoenergy to ATP and NADPH, which powers the production of carbohydrates from atmospheric CO2 and H2O. It also serves as a major production site of multivariate pro-defense molecules, and coordinate with other organelles for cell defense. Chloroplast harbors 30–50% of total cellular proteins, out of which 80% are membrane residents and are difficult to solubilize. While proteome profiling has illuminated vast areas of biological protein space, a great deal of effort must be invested to understand the proteomic landscape of the chloroplast, which plays central role in photosynthesis, energy metabolism and stress-adaptation. Therefore, characterization of chloroplast proteome would not only provide the foundation for future investigation of expression and function of chloroplast proteins, but would open up new avenues for modulation of plant productivity through synchronizing chloroplastic key components. In this review, we summarize the progress that has been made to build new understanding of the chloroplast proteome and implications of chloroplast dynamicsing generate metabolic energy and modulating stress adaptation.en_US
dc.description.sponsorshipThis work was supported by the Council of Scientific and Industrial Research (CSIR) [38/1487/ 19/EMR-II]and the Department of Biotechnology (DBT) [BT/AGR/CG-Phase II/01/2014], Govt. of India. We thank CSIR, Univresity Grants Commission (UGC) and Department of Science and Technology (DST), Govt. of India for providing research fellowship to NVL, SK, PB and DG, respectively. We sincerely apologize to all plant proteomics groups whose work could not be cited because of space constraints.en_US
dc.identifier.citationJournal of Proteomics, 212: 103542en_US
dc.identifier.doihttps://doi.org/10.1016/j.jprot.2019.103542en_US
dc.identifier.issn1874-3919
dc.identifier.officialurlhttps://www.sciencedirect.com/science/article/pii/S1874391919303148?via%3Dihuben_US
dc.identifier.urihttps://ndkr-library.nipgr.ac.in/handle/123456789/1012
dc.language.isoen_USen_US
dc.publisherElsevier B.V.en_US
dc.subjectChloroplasten_US
dc.subjectDifferentially accumulated proteinsen_US
dc.subjectKranz regulatorsen_US
dc.subjectPhotosynthetic machineryen_US
dc.subjectProteome landscapeen_US
dc.subjectStress adaptationen_US
dc.titleProteomic dissection of the chloroplast: Moving beyond photosynthesisen_US
dc.typeArticleen_US

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