Dehydration‐responsive chickpea chloroplast protein, CaPDZ1, confers dehydration tolerance by improving photosynthesis

• Published in: Physiologia plantarum 2022-01, Vol.174 (1), p.e13613-n/a
• Main Authors: Lande, Nilesh Vikram, Barua, Pragya, Gayen, Dipak, Wardhan, Vijay, Jeevaraj, Theboral, Kumar, Sunil, Chakraborty, Subhra, Chakraborty, Niranjan
• Format: Article
• Language: English
• Subjects: Assembly; Chickpeas; Chloroplast Proteins - genetics; Chloroplast Proteins - metabolism; Chloroplasts; Chloroplasts - metabolism; Cicer - genetics; Cicer - metabolism; Dehydration; Dehydration - metabolism; Domains; Eukaryotes; Oxidative stress; Photosynthesis; Photosynthesis - physiology; Photosystem II; Photosystem II Protein Complex - genetics; Photosystem II Protein Complex - metabolism; Phylogeny; Plant hormones; Protein folding; Proteins; Proteomes; Repair; Screening; Seedlings
• ISSN: 0031-9317; 1399-3054
• DOI: 10.1111/ppl.13613

The 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.