Maize opaque10 encodes a cereal-specific protein essential for the proper distribution of zeins in endosperm protein bodies
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- 英文论文题名：Maize opaque10 encodes a cereal-specific protein essential for the proper distribution of zeins in endosperm protein bodies
- 论文作者：Dongsheng Yao ; Weiwei Qi ; Xia Li ; Qing Yang ; Shumei Yan ; Huiling Ling ; Gang Wang ; Guifeng Wang ; Rentao Song
- 英文论文作者：Dongsheng Yao ; Weiwei Qi ; Xia Li ; Qing Yang ; Shumei Yan ; Huiling Ling ; Gang Wang ; Guifeng Wang ; Rentao Song ; Shanghai Key Laboratory of Bio-Energy Crops ; School of Life Sciences ; Shanghai University ; Coordinated Crop Biology Research Center (CBRC) ; National Maize Improvement Center of China ; China Agricultural University
- 年：2016
- 作者机构：Shanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University;Coordinated Crop Biology Research Center (CBRC);National Maize Improvement Center of China, China Agricultural University;
- 英文论文关键词：maize opaque mutant ; map-based cloning ; cereal-specific protein ; PB morphology ; zein distribution
- 会议召开时间：2016-10-29
- 会议录名称：第十届上海市植物生物学青年学术研讨会摘要集
- 语种：英文
- 分类号：S513
- 学会代码：ZWFZ
- 会议名称：第十届上海市植物生物学青年学术研讨会
- 会议地点：中国上海
- 主办单位：上海市植物生理与植物分子生物学学会
- 学会名称：上海市植物生理与植物分子生物学学会
- 页数：2
- 文件大小：158k
- 原文格式：D
- 会议级别：地方
摘要
Cereal storage proteins are major nitrogen source for human and livestock. Prolamins are the most abundant storage protein in most cereals. They are deposited into protein boides(PBs) in seed endosperm. So far, the inner structure and the storage mechanism for prolamin PBs remains poorly understood. Maize opaque10(o10) is a classic opaque endosperm mutant with misshapen PBs. Through positional cloning we found O10 encodes a novel cereal-specific PB protein. Its middle domain contains a seven-repeat sequence that is responsible for its dimerization. Its C-terminal of contains a transmembrane motif that is required for its ER localization and PB deposition. A cellular fractionation assay indicated that O10 is initially synthesized in the cytoplasm and then anchored to the ER, and it is eventually deposited in the PB. O10 can interact with 19-k D, 22-k D α-zeins, and 16-k D, 50-k D γ-zeins, through its N-terminal domain. The immunolocalization assay indicated that O10 co-localizes with 16-k D γ-zein and 22-k D α-zein in PB, forming a ring-shaped structure at the interface between the α-zein-rich core and the γ-zein-rich peripheral region. The loss of O10 function disrupts this ring-shaped distribution of 22-k D and 16-k D zeins, resulting in misshapen PBs. These results showed that O10, as a newly evolved PB protein, is essential for the ring-shaped distribution of 22-k D and 16-k D zeins, and controls PB morphology in maize endosperm.
Cereal storage proteins are major nitrogen source for human and livestock. Prolamins are the most abundant storage protein in most cereals. They are deposited into protein boides(PBs) in seed endosperm. So far, the inner structure and the storage mechanism for prolamin PBs remains poorly understood. Maize opaque10(o10) is a classic opaque endosperm mutant with misshapen PBs. Through positional cloning we found O10 encodes a novel cereal-specific PB protein. Its middle domain contains a seven-repeat sequence that is responsible for its dimerization. Its C-terminal of contains a transmembrane motif that is required for its ER localization and PB deposition. A cellular fractionation assay indicated that O10 is initially synthesized in the cytoplasm and then anchored to the ER, and it is eventually deposited in the PB. O10 can interact with 19-k D, 22-k D α-zeins, and 16-k D, 50-k D γ-zeins, through its N-terminal domain. The immunolocalization assay indicated that O10 co-localizes with 16-k D γ-zein and 22-k D α-zein in PB, forming a ring-shaped structure at the interface between the α-zein-rich core and the γ-zein-rich peripheral region. The loss of O10 function disrupts this ring-shaped distribution of 22-k D and 16-k D zeins, resulting in misshapen PBs. These results showed that O10, as a newly evolved PB protein, is essential for the ring-shaped distribution of 22-k D and 16-k D zeins, and controls PB morphology in maize endosperm.
Cereal storage proteins are major nitrogen source for human and livestock. Prolamins are the most abundant storage protein in most cereals. They are deposited into protein boides(PBs) in seed endosperm. So far, the inner structure and the storage mechanism for prolamin PBs remains poorly understood. Maize opaque10(o10) is a classic opaque endosperm mutant with misshapen PBs. Through positional cloning we found O10 encodes a novel cereal-specific PB protein. Its middle domain contains a seven-repeat sequence that is responsible for its dimerization. Its C-terminal of contains a transmembrane motif that is required for its ER localization and PB deposition. A cellular fractionation assay indicated that O10 is initially synthesized in the cytoplasm and then anchored to the ER, and it is eventually deposited in the PB. O10 can interact with 19-k D, 22-k D α-zeins, and 16-k D, 50-k D γ-zeins, through its N-terminal domain. The immunolocalization assay indicated that O10 co-localizes with 16-k D γ-zein and 22-k D α-zein in PB, forming a ring-shaped structure at the interface between the α-zein-rich core and the γ-zein-rich peripheral region. The loss of O10 function disrupts this ring-shaped distribution of 22-k D and 16-k D zeins, resulting in misshapen PBs. These results showed that O10, as a newly evolved PB protein, is essential for the ring-shaped distribution of 22-k D and 16-k D zeins, and controls PB morphology in maize endosperm.
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