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首页> 美国卫生研究院文献>Plant Physiology >Wild-Type Opaque2 and Defective opaque2 Polypeptides Form Complexes in Maize Endosperm Cells and Bind the Opaque2-Zein Target Site
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Wild-Type Opaque2 and Defective opaque2 Polypeptides Form Complexes in Maize Endosperm Cells and Bind the Opaque2-Zein Target Site

机译：野生型Opaque2和有缺陷的opaque2多肽在玉米胚乳细胞中形成复合物并与Opaque2-Zein靶位点结合

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The Opaque2 (O2) basic leucine (Leu)-zipper transcriptional activator controls the expression of several genes in maize (Zea mays). We investigated the phosphorylation extent of wild-type O2 and mutant-defective or mutant-truncated o2 polypeptides in endosperm cells, their subcellular localization, participation in complex formation, and involvement in functional activity. Besides wild type, four mutant alleles (o2T, o2-52, o2It, and o2-676) producing o2 polypeptides and a null transcript allele (o2R) were considered. Observing the effects of these mutations, multiphosphorylation events in O2 or o2 proteins were confirmed and further investigated, and the involvement of both the nuclear localization signal (NLS)-B and Leu-zipper domains in proper targeting to the nucleus was ascertained. The absence of these domains in the o2T and o2It-S mutant-truncated forms holds them within the cytoplasm, where they are partially phosphorylated, whereas the presence of NLS-B and a partial Leu-zipper domain in o2-52 distributes this mutant-truncated form in both cytoplasm and nucleus. Although mutated in the NLS-B domain, the o2It-L and o2-676 mutant-defective forms are, respectively, partially or completely distributed into the nucleus. Only wild-type O2 and mutant-defective o2 polypeptides bearing the Leu-zipper are able to form complexes whose components were proven to bind the O2-zein target site by in vitro analyses. The transcription of a subset of H-zein genes as well as H-zein polypeptide accumulation in several o2-mutant-defective genotypes indicate the in vivo involvement of o2-mutant-defective proteins in O2-zein target site recognition. The gathered information broadens our knowledge on O2 functional activity and our view on possible quality protein maize trait manipulation or plant transformation via the utilization of cisgenic elements.
机译：Opaque2（O2）碱性亮氨酸（Leu）拉链转录激活因子控制玉米（Zea mays）中几个基因的表达。我们调查了胚乳细胞中野生型O2和突变缺陷型或突变截短的o2多肽的磷酸化程度，它们的亚细胞定位，参与复合物形成以及参与功能活性。除野生型外，还考虑了产生o2多肽的四个突变等位基因（o2T，o2-52，o2It和o2-676）和无效的转录等位基因（o2R）。观察这些突变的影响，确认并进一步研究了O2或o2蛋白中的多磷酸化事件，并确定了核定位信号（NLS）-B和Leu-zipper域都参与了对核的正确靶向。在o2T和o2It-S突变体截短形式下，这些结构域的缺失将它们保留在细胞质中，在那里它们被部分磷酸化，而在o2-52中存在NLS-B和部分Leu拉链结构域则将这种突变体分布在细胞质中。在细胞质和细胞核中均呈截短形式。尽管在NLS-B结构域中发生了突变，但o2It-L和o2-676突变型缺陷形式分别部分或完全分布在细胞核中。只有带有Leu拉链的野生型O2和突变缺陷型o2多肽才能形成复合物，其复合物通过体外分析证明与O2-玉米醇溶蛋白靶位点结合。 H-玉米醇溶蛋白基因子集的转录以及H-玉米醇溶蛋白多肽在几种o2突变体缺陷型基因型中的积累表明o2突变体缺陷蛋白在体内参与O2玉米醇溶蛋白靶位点识别。收集到的信息拓宽了我们对O2功能活性的认识，并扩大了我们对利用顺生元素的优质玉米品质性状操纵或植物转化的认识。

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