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一些具有锌指结构域的蛋白质可以识别特定的靶RNA分子并与之结合,在细胞中参与或介导重要的生物学作用,这一发现拓展了人们对锌指蛋白专职转录调控并且高度依赖于特异结合靶DNA序列的认知。ZNF638/NP220及其同源蛋白Matrin3和RBM20是一类在生物进化中相当保守的特殊锌指蛋白,定位于细胞核基质的核斑中,含有特殊的蛋白结构域,可以特定靶向RNA分子,在细胞的转录调控和RNA加工的不同阶段发挥作用,特别是RNA转录和剪接事件的偶联以及改变RNA分子的成熟和稳定性等方面。本文将对近年来有关ZNF638同源蛋白成员的发现、结构、分子机制及其在细胞分化、胚胎发育、病毒的感染等生命过程中调控作用的研究进展进行总结讨论。 相似文献
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RRM RNA结合蛋白的结构与功能 总被引:4,自引:0,他引:4
RRM RNA结合蛋白是一类含一个或数个RRM结构域及附属结构域的RNA结合蛋白,参与RNA前体的剪接、RNA的细胞定位、RNA的稳定性等多种转录后调控过程.在RRM基序中含有许多保守的氨基酸以保证对RNA的结合活性,但是这一家族的不同蛋白质却能特异地结合各种不同的RNA分子.RRM RNA结合蛋白与某些人类遗传性疾病及肿瘤相关. 相似文献
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植物中的Dof 蛋白和Dof转录因子家族 总被引:3,自引:0,他引:3
Dof(DNA binding with one finger)蛋白是植物所特有的一类转录因子.其N末端保守的单锌指Dof结构域是既与DNA又和蛋白相互作用的双重功能域,识别的核心序列是AAAG;其C末端氨基酸序列较为多变,是Dof蛋白的特异转录调控结构域.Dof类转录因子在植物中发挥着多种功能.拟南芥和水稻的Dof转录因子家族为Aa、Bb、Cc、Dd 4个同源基因群,同类群间可能具有相似或相反的功能.文章就这一问题的研究进展作了介绍. 相似文献
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Oct-4属POU家族蛋白,是一类在动物早期胚胎发育过程中起重要作用的转录因子,参与维持细胞的全能性及未分化状态。Oct-4蛋白的主要结构特征为具有POU家族特有的保守结构域(POUS)和POU同源异型结构域(POUHD),这两个结构域可与DNA上特定区域形成双向结合,进而对基因转录进行调控。Sox-2是另一种转录因子,其HMG结构域可结合在DNA的特定序列上,并可通过与Oct-4的POUs结构域之间的蛋白质.蛋白质相互作用形成POU/HMG/DNA三元复合体以调控下游靶基因的表达。文章就POU家族成员Oct-4和HMG-box家族成员Sox-2在动物早期胚胎发育中调控部分下游基因表达的分子机制进行了概述。 相似文献
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胡杨锌指蛋白基因克隆及其结构分析 总被引:15,自引:0,他引:15
锌指蛋白属于核转录因子家族,在原核生物与真核生物基因转录调控中发挥作用。分析了耐盐锌指蛋白Alfin-1基因在苜蓿与拟南芥中的保守性后,设计了一对引物。以胡杨水培叶片为材料,从总RNA中通过RT-PCR分离得到一个锌指蛋白基因,其cDNA长924bp。分析其氨基酸序列表明,存在一个典型的Cys2/His2锌指结构,从第556位开始有一个富含G的启动子结合位点GTGGGG。由于具有相同功能的转录因子在结构和DNA结合区的氨基酸序列上具有保守性,因此,从结构分析上可以推测该基因与Alfin-1在功能上是有一定的相关性。 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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Proteins that employ dimerization domains to bind cooperatively to DNA have a number of potential advantages over monomers with regards to gene regulation. Using a combination of structure-based design and phage display, a dimeric Cys(2)His(2) zinc finger protein has been created that binds cooperatively to DNA via an attached leucine zipper dimerization domain. This chimera, derived from components of Zif268 and GCN4, displayed excellent DNA-binding specificity, and we now report the 1.5 A resolution cocrystal structure of the Zif268-GCN4 homodimer bound to DNA. This structure shows how phage display has annealed the DNA binding and dimerization domains into a single functional unit. Moreover, this chimera provides a potential platform for the creation heterodimeric zinc finger proteins that can regulate a desired target gene through cooperative DNA recognition. 相似文献
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一些在组织和细胞分化中起重要作用的蛋白质包含锌指结构域.为了克隆分离和研究与造血细胞分化和发育成熟相关的蛋白基因,利用编码C2H2型锌指蛋白结构域中部分保守氨基酸序列设计简并引物,以骨髓cDNA为模板,进行PCR扩增,得到若干新的锌指蛋白基因EST.用其中一条为探针筛选人骨髓cDNA文库,获得了一个新的锌指蛋白基因全长cDNA,GenBank收录号为AF246126,长3 888 bp,包括一个完整阅读框,编码686个氨基酸,包括17个典型的和2个非典型的C2H2模体,命名为HZF2. RNA印迹、人多组织mRNA斑点杂交分析结果显示, 其在T淋巴细胞发育和定居的器官组织胸腺、淋巴结中有较高表达,在脾脏、胎肝有中度表达,在B淋巴细胞发育的骨髓中表达很低,在外周血几个淋巴细胞系中仅有极微量的表达,提示HZF2可能对于T淋巴细胞发育和增殖有重要功能.该基因也在脑组织的若干部位、胎盘及肾上腺有较高表达,在多种其他组织细胞有微量表达,说明其可能对维持这些组织细胞的生理功能也起一定作用.将编码HZF2读框的DNA顺序克隆到pEGFP-N1载体中,转染3T3细胞,证明表达的HZF2-GFP融合蛋白定位于细胞核,这与根据HZF2蛋白结构推测其可能作为DNA结合蛋白行使调节基因转录的功能是一致的. 相似文献
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Sakai-Kato K Ishiguro A Mikoshiba K Aruga J Utsunomiya-Tate N 《Biochimica et biophysica acta》2008,1784(7-8):1011-1019
Zic family proteins have five C2H2-type zinc finger motifs. The Zic-zinc finger domains show high homology to the corresponding domains of the Gli and Glis families, which also contain five C2H2-type zinc finger motifs. The zinc finger motifs of the proteins of these three protein families form an alpha-helix conformation in solution. The addition of oligo DNA that included a Gli-binding sequence increased the alpha-helix content estimated by using circular dichroism spectroscopy. Comparison of the Zic-, Gli-, and Glis-zinc fingers indicated that the alpha-helix content after the addition of oligo DNA correlated well with the affinity of each zinc finger for the oligo DNA (correlation coefficient, 0.85). The importance of the zinc ion for protein folding was reflected in a reduction in the alpha-helix content upon removal of the zinc ion. Owing to the compact globular structure, the alpha-helix structure of the proteins of these three protein families is extremely thermally stable. These results suggest that the alpha-helix structure is important for DNA binding and profoundly related to functional and structural diversity among the three families. 相似文献