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:
影响因子:
--
通讯作者:
A. Vitale
中科院分区:
文献类型:
--
作者:
A. Pompa;A. Vitale
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.
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DOI:
10.1152/ajpcell.1999.277.1.c121
发表时间:
1999
期刊:
The American journal of physiology
影响因子:
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作者:
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DOI:
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发表时间:
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期刊:
The Plant cell
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DOI:
10.1002/j.1460-2075.1993.tb05863.x
发表时间:
1993
期刊:
The EMBO journal
影响因子:
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DOI:
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发表时间:
1994
期刊:
The Journal of biological chemistry
影响因子:
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