Retention of a Bean Phaseolin/Maize γ-Zein Fusion in the Endoplasmic Reticulum Depends on Disulfide Bond Formation[W]

Retention of a Bean Phaseolin/Maize γ-Zein Fusion in the Endoplasmic Reticulum Depends on Disulfide Bond Formation[W]
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菜豆蛋白/玉米 γ-玉米醇溶蛋白融合物在内质网中的保留取决于二硫键的形成[W]

DOI:
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发表时间:
2006
期刊:
The Plant Cell Online
影响因子:
--
通讯作者:
A. Vitale
A. Vitale
中科院分区:
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文献类型:
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作者:
A. Pompa;A. Vitale

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大多数醇溶谷蛋白类的种子贮藏蛋白在内质网(ER)中积累为称为蛋白体(PB)的大的不溶性聚合物,通过仍然知之甚少的机制。我们先前表明,菜豆液泡储存蛋白菜豆蛋白和玉米醇溶蛋白γ-玉米醇溶蛋白的N-末端半之间的融合形成ER定位的PB。沸石蛋白具有6个Cys残基,并且与具有15个残基的γ-玉米醇溶蛋白一样,除非还原,否则是不溶性的。通过研究2-巯基乙醇(2-ME)在体内的作用和通过沸石突变来确定二硫键对沸石命运的贡献。我们发现,在烟草(烟草)原生质体中,2-ME增强新合成的蛋白质与ER伴侣BiP的相互作用,并抑制可溶性蛋白质的分泌交通有或没有二硫键。尽管有这种一般的抑制作用,2-ME提高了沸石的溶解度,并减轻了其在ER中的保留,导致沸石运输增加。一致地,不能形成二硫键的突变的沸石蛋白是可溶的,并且在没有2-ME处理的情况下有效地进入分泌运输。我们的结论是,二硫键,导致不溶性是一个决定因素PB介导的蛋白质积累的ER。
Most seed storage proteins of the prolamin class accumulate in the endoplasmic reticulum (ER) as large insoluble polymers termed protein bodies (PBs), through mechanisms that are still poorly understood. We previously showed that a fusion between the Phaseolus vulgaris vacuolar storage protein phaseolin and the N-terminal half of the Zea mays prolamin γ-zein forms ER-located PBs. Zeolin has 6 Cys residues and, like γ-zein with 15 residues, is insoluble unless reduced. The contribution of disulfide bonds to zeolin destiny was determined by studying in vivo the effects of 2-mercaptoethanol (2-ME) and by zeolin mutagenesis. We show that in tobacco (Nicotiana tabacum) protoplasts, 2-ME enhances interactions of newly synthesized proteins with the ER chaperone BiP and inhibits the secretory traffic of soluble proteins with or without disulfide bonds. In spite of this general inhibition, 2-ME enhances the solubility of zeolin and relieves its retention in the ER, resulting in increased zeolin traffic. Consistently, mutated zeolin unable to form disulfide bonds is soluble and efficiently enters the secretory traffic without 2-ME treatment. We conclude that disulfide bonds that lead to insolubilization are a determinant for PB-mediated protein accumulation in the ER.
二硫键的破坏对受调节的分泌蛋白的运输表现出不同的影响。
DOI: 10.1152/ajpcell.1999.277.1.c121
发表时间: 1999
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