联会复合体的研究进展

联会复合体（ＳＣ）是性细胞减数分裂前期Ⅰ所特有的结构。其功能主要与同源染色体的配对、重组有关。已清楚,ＳＣ是由ＤＮＡ和蛋白质组成的复合体,它的形成始于细线期,完成于粗线期,它的装配和形成的每一步都是由蛋白质的合成推进。在ＳＣ中已鉴定的蛋白组分有肌动蛋白、拓扑异构酶Ⅱ和一些分子量为２６－１９０ｋＤａ的多肽。利用单抗已筛选到了某些编码ＳＣ蛋白的基因。并在重组节中证明有ＤＮＡ存在。在昆虫中ＳＣ的中心区为     

黄鳝减数分裂和联会复合体组型分析

联会复合体(Synaptonemal Complex,SC)是减数分裂前期同源染色体配对形成的一种非永久性核内细胞器,同染色体配对、遗传交换以及染色体的分离有着密切的关系。自Moses和Fawcett的早期工作以来,围绕着SC的结构、行为及化学组成等开展了大量的工作,积累了丰富的资料。近年来,由于界面铺张技术的发展,进一步推动了     

联会复合体的组成、功能及遗传控制

在多数有性生殖生物中,减数分裂第一次分裂前期同源染色体间会形成一种复杂的超级蛋白结构——联会复合体(Synaptonemal complex,SC)。该结构与同源染色体间的配对、联会、交换、分离等过程密切相关。若其出现异常,将可导致性母细胞大量凋亡,宏观上即表现为生物个体不育。近年来,该结构已成为减数分裂研究领域的一个热点,但其控制机理至今所知还十分有限。文章对联会复合体的组成、功能及其遗传控制等情况进行概述,并对其未来的研究进行探讨和展望。     

联会复合体的组成、功能及遗传控制

在多数有性生殖生物中, 减数分裂第一次分裂前期同源染色体间会形成一种复杂的超级蛋白结构--联会复合体(Synaptonemal complex, SC)。该结构与同源染色体间的配对、联会、交换、分离等过程密切相关。若其出现异常, 将可导致性母细胞大量凋亡, 宏观上即表现为生物个体不育。近年来, 该结构已成为减数分裂研究领域的一个热点, 但其控制机理至今所知还十分有限。文章对联会复合体的组成、功能及其遗传控制等情况进行概述, 并对其未来的研究进行探讨和展望。     

豚鼠精母细胞联会复合体的电镜观察

以微铺展法制备豚鼠精母细胞联会复合体标本,经硝酸银染色后作电镜观察,建立了SC组型．与有丝分裂染色体组型比较,发现二者有良好的一致性．在粗线期,X,Y轴的配对区很短,配对区的X轴和Y轴没有明显变细．未发现银染SC具有着丝粒,并对可能的原因作了分析讨论．     

中华鳖精母细胞联会复合体的研究

本文以微铺展技术制备中华鳖精母细胞联会复合体标本,经硝酸银染色后电镜观察,分析了SC组型.并与有丝分裂染色体组型相比较,发现二者有着良好的一致性,而且微小染色体的SC结构和着丝粒清晰,未发现形态上有分化的性染色体.中华鳖SC的研究为其细胞遗传学及性别决定机制提供了重要的依据.     

黑眉锦蛇的有丝分裂染色体和减数分裂联会复合体的观察

本工作以C带、硝酸银染色、对黑眉锦蛇(Elaphe taeniura)的有丝分裂染色体进行了显微观察。其二倍体染色体数目2n=36,核型组成为16(8m+6sm+2t)大染色体+20微小染色体。C带显现于几乎所有染色体的着丝粒区,有一对插入型C带位于第6对端着丝粒染色体。一个银染核仁组织区(NORs)位于No.12小染色体。同时以界面铺张——硝酸银染色技术,对黑届锦蛇减数分裂精母细胞联会复合体(SC)的结构进行了亚显微观察。发现黑眉锦蛇的SC结构与其他动物的SC相似,是由两股平行的侧线组成,SC组型与有丝分裂染色体组型有较好的一致性。     

植物减数分裂中的染色体配对、联会和重组研究进展

减数分裂是有性生殖的关键步骤,而染色体配对、联会和重组又是减数分裂的重要环节,也是减数分裂研究的热点之一。近些年来,借助于先进的分子生物学和细胞学技术,通过大量突变体的筛选,在植物减数分裂中染色体的配对、联会和重组研究取得了长足的进展。文章就目前克隆的植物减数分裂中染色体配对、联会和重组相关的基因及功能研究进行了总结,并进一步对其分子机制进行了探讨。     

Synaptonemal complex damage as a measure of genotoxicity at meiosis

Synaptonemal complex aberrations can provide a sensitive measure of chemical-specific alterations to meiotic chromosomes. Mitomycin C, cyclophosphamide, amsacrine, ellipticine, colchicine, vinblastine sulfate, and cis-platin exposures in mice have been shown to cause various patterns of synaptonemal complex structural damage and synaptic irregularity. These effects are suggestive of abnormal homologue pairing/synapsis/recombination effects which, theoretically, could be implicated in mechanisms leading to aneuploidy and other potentially heritable chromosomal disorders.     

SUMO meets meiosis: an encounter at the synaptonemal complex: SUMO chains and sumoylated proteins suggest that heterogeneous and complex interactions lie at the centre of the synaptonemal complex

Recent discoveries have identified the small ubiquitin-like modifier (SUMO) as the potential 'missing link' that could explain how the synaptonemal complex (SC) is formed during meiosis. The SC is important for a variety of chromosome interactions during meiosis and appears ladder-like. It is formed when 'axes' of the two homologous chromosomes become connected by the deposition of transverse filaments, forming the steps of the ladder. Although several components of axial and transverse elements have been identified, how the two are connected to form the SC has remained an enigma. Recent discoveries suggest that SUMO modification underlies protein-protein interactions within the SC of budding yeast. The versatility of SUMO in regulating protein-protein interactions adds an exciting new dimension to our understanding of the SC and suggests that SCs are not homogenous structures throughout the nucleus. We propose that this heterogeneity may allow differential regulation of chromosome structure and function.     

Corolla Is a Novel Protein That Contributes to the Architecture of the Synaptonemal Complex of Drosophila

In most organisms the synaptonemal complex (SC) connects paired homologs along their entire length during much of meiotic prophase. To better understand the structure of the SC, we aim to identify its components and to determine how each of these components contributes to SC function. Here, we report the identification of a novel SC component in Drosophila melanogaster female oocytes, which we have named Corolla. Using structured illumination microscopy, we demonstrate that Corolla is a component of the central region of the SC. Consistent with its localization, we show by yeast two-hybrid analysis that Corolla strongly interacts with Cona, a central element protein, demonstrating the first direct interaction between two inner-synaptonemal complex proteins in Drosophila. These observations help provide a more complete model of SC structure and function in Drosophila females.     

STAG3‐mediated stabilization of REC8 cohesin complexes promotes chromosome synapsis during meiosis

Cohesion between sister chromatids in mitotic and meiotic cells is promoted by a ring‐shaped protein structure, the cohesin complex. The cohesin core complex is composed of four subunits, including two structural maintenance of chromosome (SMC) proteins, one α‐kleisin protein, and one SA protein. Meiotic cells express both mitotic and meiosis‐specific cohesin core subunits, generating cohesin complexes with different subunit composition and possibly separate meiotic functions. Here, we have analyzed the in vivo function of STAG3, a vertebrate meiosis‐specific SA protein. Mice with a hypomorphic allele of Stag3, which display a severely reduced level of STAG3, are viable but infertile. We show that meiocytes in homozygous mutant Stag3 mice display chromosome axis compaction, aberrant synapsis, impaired recombination and developmental arrest. We find that the three different α‐kleisins present in meiotic cells show different dosage‐dependent requirements for STAG3 and that STAG3‐REC8 cohesin complexes have a critical role in supporting meiotic chromosome structure and functions.     

Fundamental cell cycle kinases collaborate to ensure timely destruction of the synaptonemal complex during meiosis

The synaptonemal complex (SC) is a proteinaceous macromolecular assembly that forms during meiotic prophase I and mediates adhesion of paired homologous chromosomes along their entire lengths. Although prompt disassembly of the SC during exit from prophase I is a landmark event of meiosis, the underlying mechanism regulating SC destruction has remained elusive. Here, we show that DDK (Dbf4‐dependent Cdc7 kinase) is central to SC destruction. Upon exit from prophase I, Dbf4, the regulatory subunit of DDK, directly associates with and is phosphorylated by the Polo‐like kinase Cdc5. In parallel, upregulated CDK1 activity also targets Dbf4. An enhanced Dbf4‐Cdc5 interaction pronounced phosphorylation of Dbf4 and accelerated SC destruction, while reduced/abolished Dbf4 phosphorylation hampered destruction of SC proteins. SC destruction relieved meiotic inhibition of the ubiquitous recombinase Rad51, suggesting that the mitotic recombination machinery is reactivated following prophase I exit to repair any persisting meiotic DNA double‐strand breaks. Taken together, we propose that the concerted action of DDK, Polo‐like kinase, and CDK1 promotes efficient SC destruction at the end of prophase I to ensure faithful inheritance of the genome.     

Synaptonemal Complex Proteins: Specific Proteins of Meiotic Chromosomes

The review considers proteins of the synaptonemal complex (SC), a specific structure formed between homologous chromosomes in maturing germline cells during meiotic prophase I. The structure and functions are described for proteins that form ultrastructural SC elements in mammals, in yeast, and in higher plants. The roles of cohesins and of the SC proteins in meiotic sister-chromatid cohesion are considered. Though still scarce, data are summarized on the SC self-assembly and dissociation and on the molecular composition of SC-associated recombination nodules, which provide a compartment for meiotic recombination enzymes. The accumulating data on the SC molecular components and on their structure, properties, and interactions improve the understanding of the SC function.     

联会复合体——原发无精症发病中的重要角色

联会复合体(synaptonemal complex,SC)是一种减数分裂特异性超分子蛋白质结构,与减数分裂I(改罗文)中同源染色体的凝缩、配对、重组和分离密切相关。近年来,联会复合体的研究取得了一系列重要的进展,包括在其组成成分和功能上的一些新发现。在小鼠不育模型中联会复合体及其编码基因的异常可引起精子发生障碍。更重要的是,联会复合体编码基因之一SCP3单个碱基缺失导致的无精症已在人类原发不育患者中得到证实。对联会复合体基因SCP1的进一步研究也正在进行之中。      

Structural analysis of the human SYCE2-TEX12 complex provides molecular insights into synaptonemal complex assembly

The successful completion of meiosis is essential for all sexually reproducing organisms. The synaptonemal complex (SC) is a large proteinaceous structure that holds together homologous chromosomes during meiosis, providing the structural framework for meiotic recombination and crossover formation. Errors in SC formation are associated with infertility, recurrent miscarriage and aneuploidy. The current lack of molecular information about the dynamic process of SC assembly severely restricts our understanding of its function in meiosis. Here, we provide the first biochemical and structural analysis of an SC protein component and propose a structural basis for its function in SC assembly. We show that human SC proteins SYCE2 and TEX12 form a highly stable, constitutive complex, and define the regions responsible for their homotypic and heterotypic interactions. Biophysical analysis reveals that the SYCE2-TEX12 complex is an equimolar hetero-octamer, formed from the association of an SYCE2 tetramer and two TEX12 dimers. Electron microscopy shows that biochemically reconstituted SYCE2-TEX12 complexes assemble spontaneously into filamentous structures that resemble the known physical features of the SC central element (CE). Our findings can be combined with existing biological data in a model of chromosome synapsis driven by growth of SYCE2-TEX12 higher-order structures within the CE of the SC.     

Sororin loads to the synaptonemal complex central region independently of meiotic cohesin complexes

The distribution and regulation of the cohesin complexes have been extensively studied during mitosis. However, the dynamics of their different regulators in vertebrate meiosis is largely unknown. In this work, we have analyzed the distribution of the regulatory factor Sororin during male mouse meiosis. Sororin is detected at the central region of the synaptonemal complex during prophase I, in contrast with the previously reported localization of other cohesin components in the lateral elements. This localization of Sororin depends on the transverse filaments protein SYCP1, but not on meiosis‐specific cohesin subunits REC8 and SMC1β. By late prophase I, Sororin accumulates at centromeres and remains there up to anaphase II. The phosphatase activity of PP2A seems to be required for this accumulation. We hypothesize that Sororin function at the central region of the synaptonemal complex could be independent on meiotic cohesin complexes. In addition, we suggest that Sororin participates in the regulation of centromeric cohesion during meiosis in collaboration with SGO2‐PP2A.