CsCHLI在茶树叶绿素生物合成中起重要作用(<i>Camellia sinensis</i>)

Yiqing Zhao, Wenjing Wang, Xihua Zhan, Mengyuan Zhang, Yao Xiao, Xinru Hou, Min Gao, Bin Xiao, Yuefang Gao
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引用次数: 0

摘要

叶绿素生物合成是植物体内重要的生物过程,叶绿素含量是影响茶叶产量和品质的重要指标之一。镁螯合酶是一种保守的叶绿素合成酶复合体,由CHLI、CHLD和CHLH亚基组成。在本研究中,CsCHLI的表达与叶绿素含量和叶绿体结构呈正相关。CsCHLI基因结构和功能域分析表明,其cDNA长度为1275 bp,编码424个氨基酸,由cTP、AAA+和AAA盖结构域组成。同时,亚细胞定位表明CsCHLI定位于叶绿体。此外,酵母双杂交(Y2H)和双分子荧光互补(BiFC)分析表明,CsCHLI可能与CsCHLI相互作用形成同型二聚体,也可能与CsCHLD和CsCHLH相互作用形成异源二聚体。此外,对拟南芥的转化表明,过表达CsCHLI可以恢复atchli1突变体的黄化表型。这些发现提供了CsCHLI在茶树叶绿素合成中的作用机制及其意义。
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CsCHLI plays an important role in chlorophyll biosynthesis of tea plant (<i>Camellia sinensis</i>)
Chlorophyll biosynthesis is a crucial biological process in plants, and chlorophyll content is one of the most important traits in the yield and quality of tea. Magnesium chelatase is a conserved enzyme complex responsible for the chlorophyll biosynthesis, which composed of the subnuit of CHLI, CHLD and CHLH. In this study, there were positive correlation between the expression of CsCHLI, chlorophyll content and chloroplast structure. The CsCHLI gene structure and functional domain indicated that, its cDNA length was 1275 bp, encodes 424 amino acids, consisted of cTP, AAA+ and AAA lid domain. Meanwhile, the subcellular localization demonstrated that CsCHLI localized in chloroplasts. In addition, protein-protein interaction analysis by yeast two-hybrid (Y2H) and bimolecular fluorescence complementation (BiFC) assays indicated that CsCHLI could interact with CsCHLI to form homodimer, or perhaps interact with CsCHLD and CsCHLH to form heterodimer. Moreover, Arabidopsis transformation displayed that overexpression of CsCHLI could restore the etiolation phenotype of the atchli1 mutant. These findings provide the mechanistic function of CsCHLI and its implications in chlorophyll biosynthesis in tea plant.
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