Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/1298
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dc.contributor.authorLande, Nilesh Vikram-
dc.contributor.authorBarua, Pragya-
dc.contributor.authorGayen, Dipak-
dc.contributor.authorWardhan, Vijay-
dc.contributor.authorJeevaraj, Theboral-
dc.contributor.authorKumar, Sunil-
dc.contributor.authorChakraborty, Subhra-
dc.contributor.authorChakraborty, Niranjan-
dc.date.accessioned2022-03-02T07:03:09Z-
dc.date.available2022-03-02T07:03:09Z-
dc.date.issued2022-
dc.identifier.citationPhysiologia Plantarum, 174(1): e13613en_US
dc.identifier.issn1399-3054-
dc.identifier.otherhttps://doi.org/10.1111/ppl.13613-
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/full/10.1111/ppl.13613-
dc.identifier.urihttp://223.31.159.10:8080/jspui/handle/123456789/1298-
dc.descriptionAccepted date: 01 December 2021en_US
dc.description.abstractThe screening of a dehydration-responsive chloroplast proteome of chickpea led us to identify and investigate the functional importance of an uncharacterized protein, designated CaPDZ1. In all, we identified 14 CaPDZs, and phylogenetic analysis revealed that these belong to photosynthetic eukaryotes. Sequence analyses of CaPDZs indicated that CaPDZ1 is a unique member, which harbours a TPR domain besides a PDZ domain. The global expression analysis showed that CaPDZs are intimately associated with various stresses such as dehydration and oxidative stress along with certain phytohormone responses. The CaPDZ1-overexpressing chickpea seedlings exhibited distinct phenotypic and molecular responses, particularly increased photosystem (PS) efficiency, ETR and qP that validated its participation in PSII complex assembly and/or repair. The investigation of CaPDZ1 interacting proteins through Y2H library screening and co-IP analysis revealed the interacting partners to be PSII associated CP43, CP47, D1, D2 and STN8. These findings supported the earlier hypothesis regarding the role of direct or indirect involvement of PDZ proteins in PS assembly or repair. Moreover, the GUS-promoter analysis demonstrated the preferential expression of CaPDZ1 specifically in photosynthetic tissues. We classified CaPDZ1 as a dehydration-responsive chloroplast intrinsic protein with multi-fold abundance under dehydration stress, which may participate synergistically with other chloroplast proteins in the maintenance of the photosystem.en_US
dc.description.sponsorshipThis work was supported by grants from the Department of Biotech-nology (DBT), India (BT/AGR/CG-PhaseII/01/2014) and the NationalInstitute of Plant Genome Research, New Delhi to NiranjanChakraborty. The authors thank the Council of Scientific and Indus-trial Research (CSIR), India for providing a pre-doctoral fellowship toNilesh Vikram Lande. They also sincerely acknowledge the Depart-ment of Biotechnology (DBT) for providing a pre-doctoral fellowshipto Sunil Kumar. They also thank Mr. Jasbeer Singh for the illustrationsand graphical representation in the manuscript.en_US
dc.language.isoen_USen_US
dc.publisherJohn Wiley & Sonsen_US
dc.subjectchickpea chloroplast proteinen_US
dc.subjectdehydration toleranceen_US
dc.subjectphotosynthesisen_US
dc.subjectCaPDZ1en_US
dc.titleDehydration-responsive chickpea chloroplast protein, CaPDZ1, confers dehydration tolerance by improving photosynthesisen_US
dc.typeArticleen_US
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