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植物C_2H_2型锌指蛋白的研究进展 总被引:2,自引:0,他引:2
锌指蛋白是转录因子的一种,对真核生物的生长发育及逆境胁迫的耐受能力都有着重要关系,而植物C2H2型锌指蛋白是研究较多、较为明确的一种锌指蛋白,该蛋白大部分锌指结构具有一段高度保守的氨基酸序列QALGGH,这是植物中独有的特征,且据报道该C2H2型锌指蛋白与逆境胁迫是相关的。本文主要综述了植物C2H2型锌指蛋白的分类、结构和功能,植物C2H2型锌指蛋白与DNA、RNA和蛋白质的相互作用,以及概述了与盐胁迫、低温胁迫、干旱胁迫、氧胁迫和光胁迫等逆境胁迫相关的植物C2H2型锌指蛋白,最后还对其进一步的深入研究进行了展望,这就为日后利用基因工程技术改良作物品质、提高作物的抗逆性提供了有利条件。 相似文献
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C2H2锌指是真核细胞中最常见的DNA结合模体。由于C2H2锌指域靶位点特异性与结构和功能的模块性构成,使得C2H2锌指域成为构建特定的DNA结合蛋白的常用骨架。保持C2H2锌指的基本骨架不变,替换锌指特定位点的氨基酸残基,并融合表达其他功能域就可以得到具有靶向性的人造锌指蛋白(ZFP)。ZFP可以介导靶基因的转录调控,抑制或激活特定基因的表达与配体依赖的靶基因激活或抑制;对DNA进行修饰,如人造限制性内切酶,重组酶,整合酶;抗病毒感染等。因此,人造锌指蛋白应用前景广阔,研究价值显著,是未来人类基因治疗的革命性的工具。 相似文献
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C2H2型锌指蛋白的研究进展 总被引:2,自引:0,他引:2
锌指基因家族是人体中最大的基因家族,它参与细胞分化、胚胎发育,并与许多疾病的发生相关.根据半胱氨酸(c)和组氨酸(H)的数目和位置可将锌指蛋白分为c2H2、c2Hc2、c2c2 CHCC2C2、C2C2C2C2等亚类.c2H2型锌指是最普遍的类型,它们作为重要的转录调控因子参与许多的生理过程.c2H2型锌指蛋白包含的锌指数目从1个到30多个不等.依据锌指的数量以及在蛋白中的分布情况,大多数c2H2型锌指蛋白属于下列3类之一:1)含3个c:H:锌指的蛋白(tC2H2);2)含多个锌指的c2H2型锌指结构蛋白(mac2H2);3)锌指成对间隔排列的c2H2型锌指蛋白(spC2H2)、一些c2H2型锌指蛋白能识别并结合特异性RNA或DNA片段.另一些则只能与RNA结合.通常锌指蛋白含锌指数目越多。它选择结合的能力就越强. 相似文献
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C2H2锌指蛋白转录因子家族在真核生物中具有重要的生物学功能,广泛参与植物叶的发生、花器官的调控、侧枝的形成及逆境胁迫等生命过程。植物C2H2锌指蛋白不仅结合DNA和RNA,而且与蛋白质之间相互作用。本研究利用普通烟草(Nicotiana tabacum)基因组数据库,运用Blastp比对,结合Pfam和SMART分析,鉴定了118条普通烟草C2H2锌指蛋白家族成员;对烟草C2H2锌指蛋白家族进行了进化树分析、结构域分析、物理化学性质分析、染色体定位、基因结构分析、三维结构分析及组织表达分析等。结果表明:不同成员的氨基酸长度差异较大;系统进化及结构域分析显示,所有C2H2家族成员可以被分为5个亚家族,同一亚家族成员之间在结构域和理化性质上呈现较高一致性;每个成员都含有C2H2结构域,在数量上存在较大差异;将所有基因家族成员定位在22条染色体上;组织表达分析表明,每个C2H2亚家族都有成员在不同组织中表达,在叶及根中有些基因的表达量较高。 相似文献
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锌簇家族蛋白即Zn2Cys6类锌指蛋白,是真菌中特有的一类蛋白,它们属于转录因子类,广泛参与真菌中初级和次级代谢、胁迫应答和细胞分裂等生命活动的调控。锌簇蛋白主要包括N端的DNA结合结构域、中间的调节结构域和C端的酸性区域,其中DNA结合结构域包含锌指基序并负责结合靶基因的启动子。目前已经解析了多个锌簇家族转录因子DNA结合结构域的三维结构,并发现该家族中一些蛋白能够参与调控多个基因的表达,但缺乏对其结构、动力学和功能关系的全面分析。本文综合分析了不同锌簇蛋白与DNA结合的结构特征,总结其结构域与功能的关系,指出锌簇蛋白研究的重要方向,旨在为锌簇家族蛋白的深入研究提供思路。 相似文献
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Cys2-His2 (C2H2) zinc finger domains (ZFs) were originally identified as DNA-binding domains, and uncharacterized domains
are typically assumed to function in DNA binding. However, a growing body of evidence suggests an important and widespread
role for these domains in protein binding. There are even examples of zinc fingers that support both DNA and protein interactions,
which can be found in well-known DNA-binding proteins such as Sp1, Zif268, and Ying Yang 1 (YY1). C2H2 protein–protein interactions
(PPIs) are proving to be more abundant than previously appreciated, more plastic than their DNA-binding counterparts, and
more variable and complex in their interactions surfaces. Here we review the current knowledge of over 100 C2H2 zinc finger-mediated
PPIs, focusing on what is known about the binding surface, contributions of individual fingers to the interaction, and function.
An accurate understanding of zinc finger biology will likely require greater insights into the potential protein interaction
capabilities of C2H2 ZFs. 相似文献
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There are over 10,000 C2H2-type zinc finger (ZF) domains distributed among more than 1,000 ZF proteins in the human genome. These domains are frequently observed to be involved in sequence-specific DNA binding, and uncharacterized domains are typically assumed to facilitate DNA interactions. However, some ZFs also facilitate binding to proteins or RNA. Over 100 Cys2-His2 (C2H2) ZF-protein interactions have been described. We initially attempted a bioinformatics analysis to identify sequence features that would predict a DNA- or protein-binding function. These efforts were complicated by several issues, including uncertainties about the full functional capabilities of the ZFs. We therefore applied an unbiased approach to directly examine the potential for ZFs to facilitate DNA or protein interactions. The human OLF-1/EBF associated zinc finger (OAZ) protein was used as a model. The human O/E-1-associated zinc finger protein (hOAZ) contains 30 ZFs in 6 clusters, some of which have been previously indicated in DNA or protein interactions. DNA binding was assessed using a target site selection (CAST) assay, and protein binding was assessed using a yeast two-hybrid assay. We observed that clusters known to bind DNA could facilitate specific protein interactions, but clusters known to bind protein did not facilitate specific DNA interactions. Our primary conclusion is that DNA binding is a more restricted function of ZFs, and that their potential for mediating protein interactions is likely greater. These results suggest that the role of C2H2 ZF domains in protein interactions has probably been underestimated. The implication of these findings for the prediction of ZF function is discussed. 相似文献
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