Leaf senescence is one of the major factors contributing to the productivity and the grain quality in crops. The regulatory mechanism of leaf senescence remains largely unknown. Here, we report the identification and ...Leaf senescence is one of the major factors contributing to the productivity and the grain quality in crops. The regulatory mechanism of leaf senescence remains largely unknown. Here, we report the identification and characterization of a rice e_aarly senescence 1 （easl） mutant, which displayed an early leaf senescence phenotype, accompanying by dwarfism and reduced tiller number, eventually leading to the reduction of grain yield. Map-based cloning revealed that the nuclear gene EAS1 encodes a pheophorbide a oxygenase （PaO）, a key enzyme for chlorophyll breakdown. A highly conserved Thr residue of PaO was mutated into Ile in the easl mutant. Phylogenetic analysis indicates that PaO is an evolutionarily conserved protein, and EAS1 is 68% identical to the Arabidopsis ACCERLERATED CELL DEATH （ACD1） protein. Unlike ACD1 that contains a single transit peptide, EAS1 contains two putative transit peptides at its N-ter- minus, which are essential for its functionality, suggesting that targeting of EAS1 to the chloroplast is likely mediated by a putative bipartite transit peptide. Consistently, only a short version of EAS1 lacking the first putative transit peptide, but not the full-length EAS1, was capable of rescuing the Arabidopsis acdl mutant phenotype. These results suggest that rice EASI represents a functional PaO, which is involved in chlorophyl/degradation and may utilize a unique mechanism for its import into the chloroplast.展开更多
基金supported by grants from Chinese Academy of Sciences (No. XDA0801040102)National Natural Science Foundation of China (No. 30770209)State Key Laboratory of Plant Genomics (No. SKLPG2011A0210)
文摘Leaf senescence is one of the major factors contributing to the productivity and the grain quality in crops. The regulatory mechanism of leaf senescence remains largely unknown. Here, we report the identification and characterization of a rice e_aarly senescence 1 （easl） mutant, which displayed an early leaf senescence phenotype, accompanying by dwarfism and reduced tiller number, eventually leading to the reduction of grain yield. Map-based cloning revealed that the nuclear gene EAS1 encodes a pheophorbide a oxygenase （PaO）, a key enzyme for chlorophyll breakdown. A highly conserved Thr residue of PaO was mutated into Ile in the easl mutant. Phylogenetic analysis indicates that PaO is an evolutionarily conserved protein, and EAS1 is 68% identical to the Arabidopsis ACCERLERATED CELL DEATH （ACD1） protein. Unlike ACD1 that contains a single transit peptide, EAS1 contains two putative transit peptides at its N-ter- minus, which are essential for its functionality, suggesting that targeting of EAS1 to the chloroplast is likely mediated by a putative bipartite transit peptide. Consistently, only a short version of EAS1 lacking the first putative transit peptide, but not the full-length EAS1, was capable of rescuing the Arabidopsis acdl mutant phenotype. These results suggest that rice EASI represents a functional PaO, which is involved in chlorophyl/degradation and may utilize a unique mechanism for its import into the chloroplast.
