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Characterization and fine mapping of the rice premature senescence mutant ospse1

文献类型: 外文期刊

作者: Wu, Hai-Bin 1 ; Wang, Bin 1 ; Chen, Yuanling 1 ; Liu, Yao-Guang 1 ; Chen, Letian 1 ;

作者机构: 1.South China Agr Univ, State Key Lab Conservat & Utilizat Subtrop Agrobi, Coll Life Sci, Guangzhou 510642, Guangdong, Peoples R China

2.Guangdong Acad Agr Sci, Vegetable Res Inst, Guangzhou 510640, Peoples R China

3.South China Agr Univ, Guangdong Prov Key Lab Prot Funct & Regulat Agr O, Coll Life Sci, Guangzhou 510642, Guangdong, Peoples R China

期刊名称:THEORETICAL AND APPLIED GENETICS ( 影响因子:5.699; 五年影响因子:5.565 )

ISSN: 0040-5752

年卷期: 2013 年 126 卷 7 期

页码:

收录情况: SCI

摘要: Premature senescence can limit crop productivity by limiting the growth phase. In the present study, a spontaneous premature senescence mutant was identified in rice (Oryza sativa L.). Genetic analysis revealed that the premature senescence phenotype was controlled by a recessive mutation, which we named Oryza sativa premature senescence1 (ospse1). The ospse1 mutants showed premature leaf senescence from the booting stage and exhibited more severe symptoms during reproductive and ripening stages. Key yield-related agronomic traits such as 1,000-grain weight and seed-setting rate, but not panicle grain number, were significantly reduced in ospse1 plants. Chlorophyll content, net photosynthetic rate, and transpiration rate of ospse1 flag leaves were similar to the wild-type plants in vegetative stages, but these parameters decreased steeply in the mutant after the heading stage. Consistent with this, the senescence-associated genes OsNYC1 and OsSgr were up-regulated in ospse1 mutant during premature leaf senescence. The ospse1 locus was mapped to a 38-kb region on chromosome 1 and sequence analysis of this region identified a single-nucleotide deletion in the 3' region of an open reading frame (ORF) encoding a putative pectate lyase, leading to a frame shift and a longer ORF. Our results suggested that the premature senescence of the ospse1 may be regulated by a novel mechanism mediated by pectate lyase.

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