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在豆科植物豇豆中发现了三种不同植物铁蛋白亚基的功能基因。

Functional genes found for three different plant ferritin subunits in the legume, Vigna unguiculata.

作者信息

Wicks R E, Entsch B

机构信息

Department of Biochemistry, Microbiology, and Nutrition, University of New England, Armidale, NSW, Australia.

出版信息

Biochem Biophys Res Commun. 1993 Apr 30;192(2):813-9. doi: 10.1006/bbrc.1993.1487.

DOI:10.1006/bbrc.1993.1487
PMID:8484787
Abstract

The iron storage protein, ferritin, in plants can occur in multiple molecular forms that, until now, were proposed to be derived from degradation of a single mature polypeptide subunit (2,7,17), which is assembled into the holoprotein and functions in plastids. We have carried out some definitive experiments with the diploid legume, Vigna unguiculata (cowpeas), which show that there are functioning genes for three different ferritin subunits in the developing leaves. Unique segments of mRNAs which code for subunits with substantially different mature sequences were detected by PCR. Separate genes for each subunit were found by showing that each gene contained a unique intron. Thus, multiple molecular forms of ferritin can arise through differential expression of a family of genes in plants.

摘要

植物中的铁储存蛋白铁蛋白可以以多种分子形式存在,直到现在,人们认为这些形式是由单个成熟多肽亚基降解产生的(2,7,17),该亚基组装成全蛋白并在质体中发挥作用。我们对二倍体豆科植物豇豆进行了一些确定性实验,结果表明,在发育中的叶片中存在三种不同铁蛋白亚基的功能基因。通过PCR检测到编码具有显著不同成熟序列亚基的mRNA的独特片段。通过证明每个基因都包含一个独特的内含子,发现了每个亚基的单独基因。因此,铁蛋白的多种分子形式可以通过植物中一个基因家族的差异表达产生。

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Biochem Biophys Res Commun. 1993 Apr 30;192(2):813-9. doi: 10.1006/bbrc.1993.1487.
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Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin.植物铁蛋白的晶体结构揭示了一个新的金属结合位点,该位点在铁蛋白中作为金属转移的过渡位点发挥作用。
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Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation.有证据表明,暴露在三重通道上的残基在铁蛋白铁掺入机制中发挥着积极作用。
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