共查询到19条相似文献,搜索用时 140 毫秒
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李伟 《中国生物工程杂志》2011,31(11):1-5
PLZF(promyelocytic leukaemia zinc finger protein)是一种重要的转录抑制因子,它由位于N端的BTB结构域和C端的锌指结构域构成。鉴于目前对于锌指结构域的立体结构还不是十分清楚,对其进行了高效表达和提纯。为了表达PLZF蛋白的锌指结构域,在其编码序列的5'端加上起始密码ATG后插入到表达载体PET-11a的多克隆位点。构建好的表达质粒转化到BL21 (DE3)大肠杆菌内并用IPTG诱导表达,发现重组蛋白主要以不溶性的包涵体形式在胞内表达。用含有SDS变性剂的缓冲液溶解包涵体后,采用凝胶过滤方法将重组蛋白纯化到纯度达96%以上。对纯化后的蛋白质用反透析的方法进行复性,然后用DNA结合实验进行活性分析,发现复性后的蛋白质具有特异的DNA结合活性,这为进一步研究PLZF蛋白锌指结构域的立体结构打下了重要基础。 相似文献
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真核生物中锌指蛋白的结构与功能 总被引:3,自引:0,他引:3
真核生物中的许多蛋白质分子包含锌指结构区,这类蛋白称为锌指蛋白.锌指蛋白因其包含特殊的指状结构,在对DNA、蛋白质和RNA的识别和结合中起重要作用.许多锌指蛋白的锌指结构域包含能与DNA特异结合的区域,并与某些效应结构域(如KRAB、SCAN、BTB/POZ、SNAG、SANT和PLAG等)相连,这类锌指蛋白常作为转录因子起作用,可调控靶基因的转录.一些锌指蛋白包含蛋白质识别结构域(如LIM锌指、MYND锌指、PHD锌指和RING锌指等),它们能够特异地介导蛋白质之间的相互作用,因此被称作蛋白适配器.此外,某些锌指蛋白还可以结合RNA,起转录后调控作用.本文就锌指蛋白与DNA、RNA以及蛋白质分子间的相互作用作一综述. 相似文献
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Prdm1(PR domain zinc finger protein 1),又称为Blimpl(B—lymphocyte-induced maturation protein-1),是一个具有锌指结构的转录因子,通过调控多个基因的表达影响哺乳动物多种类型细胞的发育分化。从1991年发现至今,有关Prdm1的研究进展迅速,Prdm1在促进B细胞向浆细胞终末分化过程中的作用已经得到共识。但是,在小鼠及其他哺乳动物的胚胎发育过程中,尤其是关于Prdm1在生殖细胞发育分化中的作用机理研究则起步相对较晚。近期发现,在哺乳动物胚胎发育过程中,Prdm1在原始生殖细胞的形成、干细胞全能性的维持以及其他组织器官的形成中都发挥了重要的作用。 相似文献
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POZ锌指蛋白是一类在进化中高度保守的蛋白,具有多种重要的生物学功能。POZ锌指蛋白主要作为一种转录抑制因子而存在,通过POZ结构域招募一些转录辅阻遏物而调节靶基因的表达。近年来的研究发现,POZ锌指蛋白在发育和肿瘤的发生中有着重要的作用,综述5个POZ锌指蛋白在肿瘤的发生和生物体发育中的作用及功能,为人们进一步了解POZ锌指蛋白的功能提供资料。 相似文献
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锌指蛋白(zinc finger protein,ZNF/ZFP)是一类具有手指状结构域的转录因子,广泛存在于动、植物及微生物体内。ZNF在多种肿瘤组织中表达,通过调控下游靶基因的表达参与肿瘤的发生发展过程。ZNF表达异常与结直肠癌临床病理特征和预后密切相关。本文从结直肠癌的增殖、迁移和侵袭、凋亡、癌细胞干性等4种恶性行为角度,阐述了近年来锌指蛋白家族成员(ZEB1/2、Gli1/3、PLAGL1/2、KLF4、Snail1、ZBTB7A、ZBTB7C、ZBTB16)在结直肠癌中的作用机制,旨在为临床靶向治疗结直肠癌提供参考依据。 相似文献
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In-depth mutational analysis of the promyelocytic leukemia zinc finger BTB/POZ domain reveals motifs and residues required for biological and transcriptional functions 总被引:12,自引:0,他引:12 下载免费PDF全文
Melnick A Ahmad KF Arai S Polinger A Ball H Borden KL Carlile GW Prive GG Licht JD 《Molecular and cellular biology》2000,20(17):6550-6567
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In acute promyelocytic leukemia (APL), hematopoietic differentiation is blocked and immature blasts accumulate in the bone marrow and blood. APL is associated with chromosomal aberrations, including t(15;17) and t(11;17). For these two translocations, the retinoic acid receptor alpha (RARα) is fused to the promyelocytic leukemia (PML) gene or the promyelocytic zinc finger (PLZF) gene, respectively. Both fusion proteins lead to the formation of a high-molecular-weight complex. High-molecular-weight complexes are caused by the “coiled-coil” domain of PML or the BTB/POZ domain of PLZF. PML/RARα without the “coiled-coil” fails to block differentiation and mediates an all-trans retinoic acid-response. Similarly, mutations in the BTB/POZ domain disrupt the high-molecular-weight complex, abolishing the leukemic potential of PLZF/RARα. Specific interfering polypeptides were used to target the oligomerization domain of PML/RARα or PLZF/RARα. PML/RARα and PLZF/RARα were analyzed for the ability to form high-molecular-weight complexes, the protein stability and the potential to induce a leukemic phenotype in the presence of the interfering peptides. Expression of these interfering peptides resulted in a reduced replating efficiency and overcame the differentiation block induced by PML/RARα and PLZF/RARα in murine hematopoietic stem cells. This expression also destabilized the PLZF/RARα-induced high-molecular-weight complex formation and caused the degradation of the fusion protein. Targeting fusion proteins through interfering peptides is a promising approach to further elucidate the biology of leukemia. 相似文献
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Cathy Mitchelmore Karen M Kjaerulff Hans C Pedersen Jakob V Nielsen Thomas E Rasmussen Mads F Fisker Bente Finsen Karen M Pedersen Niels A Jensen 《The Journal of biological chemistry》2002,277(9):7598-7609
BTB/POZ (broad complex tramtrack bric-a-brac/poxvirus and zinc finger) zinc finger factors are a class of nuclear DNA-binding proteins involved in development, chromatin remodeling, and cancer. However, BTB/POZ domain zinc finger factors linked to development of the mammalian cerebral cortex, cerebellum, and macroglia have not been described previously. We report here the isolation and characterization of two novel nuclear BTB/POZ domain zinc finger isoforms, designated HOF(L) and HOF(S), that are specifically expressed in early hippocampal neurons, cerebellar granule cells, and gliogenic progenitors as well as in differentiated glia. During embryonic development of the murine cerebral cortex, HOF expression is restricted to the hippocampal subdivision. Expression coincides with early differentiation of presumptive CA1 and CA3 pyramidal neurons and dentate gyrus granule cells, with a sharp decline in expression at the CA1/subicular border. By using bromodeoxyuridine labeling and immunohistochemistry, we show that HOF expression coincides with immature non-dividing cells and is down-regulated in differentiated cells, suggesting a role for HOF in hippocampal neurogenesis. Consistent with the postulated role of the POZ domain as a site for protein-protein interactions, both HOF isoforms are able to dimerize. The HOF zinc fingers bind specifically to the binding site for the related promyelocytic leukemia zinc finger protein as well as to a newly identified DNA sequence. 相似文献
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The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein 总被引:11,自引:0,他引:11 下载免费PDF全文
Melnick AM Westendorf JJ Polinger A Carlile GW Arai S Ball HJ Lutterbach B Hiebert SW Licht JD 《Molecular and cellular biology》2000,20(6):2075-2086