Abstract

The filamentation temperature-sensitive H (FtsH) metalloprotease participates in the chloroplast photosystem II (PSII) repair cycle, playing a crucial role in regulating leaf coloration. However, the evolutionary history and biological function of the FtsH family in albino tea plants are still unknown. In this study, 35 CsFtsH members, including 7 CsFtsH-like (CsFtsHi1-CsFtsHi7) proteins, mapping onto 11 chromosomes in 6 subgroups, were identified in the ‘Shuchazao2′ tea genome, and their exon/intron structure, domain characteristics, collinearity, protein interaction network, and secondary structure were comprehensively analyzed. Furthermore, real-time fluorescence quantitative PCR (RT-qPCR) analysis revealed that the expression levels of CsFtsH1/2/5/8 were significantly positively correlated with the leaf color of tea plants. The subcellular localization revealed that they were located in the chloroplast. The transgenic Arabidopsis has demonstrated that CsFtsH2 and CsFtsH5 could restore the chlorophyll content and chlorophyll fluorescence intensity in var1 and var2 mutants, respectively. Moreover, protein–protein interactions have confirmed that CsFtsH1 with CsFtsH5, and CsFtsH2 with CsFtsH8 could form a hetero-comples and function in chloroplasts. In summary, this study aims to not only increase the understanding of the underlying molecular mechanisms of CsFtsH but also to provide a solid and detailed theoretical foundation for the breeding of albino tea plant varieties.

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