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1.
THE STRUCTURE OF THE CENTRAL REGION IN THE SYNAPTONEMAL COMPLEXES OF HAMSTER AND CRICKET SPERMATOCYTES 总被引:5,自引:3,他引:2
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The fine structure of bivalents from golden hamster and house cricket spermatocytes has been studied with a whole mount surface-spreading method combined with negative staining. The elements of the synaptonemal complex show detail of structure which is absent in other preparative procedures. The transverse filaments found in the central region of the synaptonemal complex from both species are straight and have a similar width, 1 6–1 8 nm These filaments occur mainly in bundles The central element differs in architecture in the two species In hamster bivalents it is formed of longitudinal stretches of filaments 1.6–1 8 nm wide and a small amount of an amorphous material similar to that of the lateral elements In the cricket, the central element contains transverse fibrils which are continuous with the transverse filaments of the central region, and an amorphous material lying mainly along the sides of the central element All of the components of the central region of the synaptonemal complex are resistant to pancreatic DNase. The overlapping ends of the transverse filaments, together with additional protein material, make up the central element The widespread occurrence and close morphological and histochemical interspecies similarities of the transverse filaments indicate that they serve an essential role, probably one concerned with holding synapsed bivalents together via the lateral elements. Restrictions placed by the observations reported here on current models of the synaptonemal complex are discussed. 相似文献
2.
Watts FZ Hoffmann E 《BioEssays : news and reviews in molecular, cellular and developmental biology》2011,33(7):529-537
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. 相似文献
3.
Heyting C 《Transgenic research》2005,14(5):547-550
Meiosis is a specialized set of two nuclear divisions, meiosis I and II, by which a diploid cell produces four haploid daughters.
After premeiotic DNA replication, homologous chromosomes pair and recombine, and then disjoin at meiosis I. Subsequently,
at meiosis II, the sister chromatids of each chromosome segregate. In nearly all eukaryotes, meiotic chromosome pairing culminates
in the formation of a ladderlike supramolecular protein structure, the synaptonemal complex (SC) (Page and Hawley, 2004).
The rungs of the ladder are known as transverse filaments (TFs). Genes encoding TF proteins have been identified in a limited
number of organisms, and their function has been studied by mutational analysis. Although TF proteins show little amino acid
sequence conservation, their structure and function are largely conserved. In all analyzed species, TF proteins are required
for meiotic reciprocal recombination (crossing over). 相似文献
4.
The Synaptonemal Complex Protein SCP3 Can Form Multistranded, Cross-striated Fibers In Vivo 总被引:13,自引:2,他引:11
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Li Yuan Jeanette Pelttari Eva Brundell Birgitta Bjrkroth Jian Zhao Jian-Guo Liu Hjalmar Brismar Bertil Daneholt Christer Hg 《The Journal of cell biology》1998,142(2):331-339
The synaptonemal complex protein SCP3 is part of the lateral element of the synaptonemal complex, a meiosis-specific protein structure essential for synapsis of homologous chromosomes. We have investigated the fiber-forming properties of SCP3 to elucidate its role in the synaptonemal complex. By synthesis of SCP3 in cultured somatic cells, it has been shown that SCP3 can self-assemble into thick fibers and that this process requires the COOH-terminal coiled coil domain of SCP3, as well as the NH2-terminal nonhelical domain. We have further analyzed the thick SCP3 fibers by transmission electron microscopy and immunoelectron microscopy. We found that the fibers display a transversal striation with a periodicity of ~20 nm and consist of a large number of closely associated, thin fibers, 5–10 nm in diameter. These features suggest that the SCP3 fibers are structurally related to intermediate filaments. It is known that in some species the lateral elements of the synaptonemal complex show a highly ordered striated structure resembling that of the SCP3 fibers. We propose that SCP3 fibers constitute the core of the lateral elements of the synaptonemal complex and function as a molecular framework to which other proteins attach, regulating DNA binding to the chromatid axis, sister chromatid cohesion, synapsis, and recombination. 相似文献
5.
6.
A Meiotic Chromosomal Core Consisting of Cohesin Complex Proteins Recruits DNA Recombination Proteins and Promotes Synapsis in the Absence of an Axial Element in Mammalian Meiotic Cells 总被引:25,自引:0,他引:25
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Jeanette Pelttari Mary-Rose Hoja Li Yuan Jian-Guo Liu Eva Brundell Peter Moens Sabine Santucci-Darmanin Rolf Jessberger Jose Luis Barbero Christa Heyting Christer Hg 《Molecular and cellular biology》2001,21(16):5667-5677
The behavior of meiotic chromosomes differs in several respects from that of their mitotic counterparts, resulting in the generation of genetically distinct haploid cells. This has been attributed in part to a meiosis-specific chromatin-associated protein structure, the synaptonemal complex. This complex consist of two parallel axial elements, each one associated with a pair of sister chromatids, and a transverse filament located between the synapsed homologous chromosomes. Recently, a different protein structure, the cohesin complex, was shown to be associated with meiotic chromosomes and to be required for chromosome segregation. To explore the functions of the two different protein structures, the synaptonemal complex and the cohesin complex, in mammalian male meiotic cells, we have analyzed how absence of the axial element affects early meiotic chromosome behavior. We find that the synaptonemal complex protein 3 (SCP3) is a main determinant of axial-element assembly and is required for attachment of this structure to meiotic chromosomes, whereas SCP2 helps shape the in vivo structure of the axial element. We also show that formation of a cohesin-containing chromosomal core in meiotic nuclei does not require SCP3 or SCP2. Our results also suggest that the cohesin core recruits recombination proteins and promotes synapsis between homologous chromosomes in the absence of an axial element. A model for early meiotic chromosome pairing and synapsis is proposed. 相似文献
7.
Sororin loads to the synaptonemal complex central region independently of meiotic cohesin complexes
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Rocío Gómez Natalia Felipe‐Medina Miguel Ruiz‐Torres Inés Berenguer Alberto Viera Sara Pérez José Luis Barbero Elena Llano Tomoyuki Fukuda Manfred Alsheimer Alberto M Pendás Ana Losada José A Suja 《EMBO reports》2016,17(5):695-707
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. 相似文献
8.
The synaptonemal complex (SC) in the beetleBlaps cribrosa contains a highly organized central element (CE), two flanking lateral elements (LEs), and a number of regularly spaced transverse filaments (TFs) crossing the central region. The CE is built like a ladder with two longitudinal components running in parallel and a number of regularly spaced transverse CE components, briding the two longitudinal components. The CE is multi-layered with the ladders of the individual layers more or less in register. Essentially every TF originates in one of the LEs, crosses the CE through a transverse CE component and reaches the opposite LE; every transverse CE component in a given layer corresponds to one, and only one, TF. In a CE layer, short irregular pillars form the junctions between the transverse and longitudinal CE components. Adjacent pillars are connected to each other by fine fibrous bridges: the two pillars in the same transverse CE component are linked, and so are the pillars along each longitudinal component, and also more occasionally adjacent pillars in separate CE layers. It is proposed that a TF with the two associated short pillars represents the structural unit in the central region. The ordered structure of the CE is accomplished by linking adjacent pillars to each other into the well-defined three-dimensional organization of the CE. 相似文献
9.
In most eukaryotes, homologous chromosomes (homologs) are closely apposed during the prophase of the first meiotic division by a ladderlike proteinaceous structure, the synaptonemal complex (SC) [Fawcett, J Biophys Biochem Cytol 2:403–406, 1956; Moses, J Biophys Biochem Cytol 2:215–218, 1956]. SCs consist of two proteinaceous axes, which each support the two sister chromatids of one homolog, and numerous transverse filaments (TFs), which connect the two axes. Organisms that assemble SCs perform meiotic recombination in the context of these structures. Although much information has accumulated about the composition of SCs and the pathways of meiotic crossing over, several questions remain about the role of SCs in meiosis, in particular, about the role of the TFs. In this review, we focus on possible role(s) of TFs. The interest in TF functions received new impulses from the recent characterization of TF-deficient mutants in a number of species. Intriguingly, the phenotypes of these mutants are very different, and a variety of TF functions appear to be hidden behind a façade of morphological conservation. However, in all TF-deficient mutants a specific class of crossovers that display interference is affected. TFs appear to create suitable preconditions for the formation of these crossovers in most species, but are most likely not directly involved in the interference process itself. Furthermore, TFs are important for full-length homolog alignment.The synaptonemal complex—50 years. 相似文献
10.
Bisig CG Guiraldelli MF Kouznetsova A Scherthan H Höög C Dawson DS Pezza RJ 《PLoS genetics》2012,8(6):e1002701
Recent studies in simple model organisms have shown that centromere pairing is important for ensuring high-fidelity meiotic chromosome segregation. However, this process and the mechanisms regulating it in higher eukaryotes are unknown. Here we present the first detailed study of meiotic centromere pairing in mouse spermatogenesis and link it with key events of the G2/metaphase I transition. In mouse we observed no evidence of the persistent coupling of centromeres that has been observed in several model organisms. We do however find that telomeres associate in non-homologous pairs or small groups in B type spermatogonia and pre-leptotene spermatocytes, and this association is disrupted by deletion of the synaptonemal complex component SYCP3. Intriguingly, we found that, in mid prophase, chromosome synapsis is not initiated at centromeres, and centromeric regions are the last to pair in the zygotene-pachytene transition. In late prophase, we first identified the proteins that reside at paired centromeres. We found that components of the central and lateral element and transverse filaments of the synaptonemal complex are retained at paired centromeres after disassembly of the synaptonemal complex along diplotene chromosome arms. The absence of SYCP1 prevents centromere pairing in knockout mouse spermatocytes. The localization dynamics of SYCP1 and SYCP3 suggest that they play different roles in promoting homologous centromere pairing. SYCP1 remains only at paired centromeres coincident with the time at which some kinetochore proteins begin loading at centromeres, consistent with a role in assembly of meiosis-specific kinetochores. After removal of SYCP1 from centromeres, SYCP3 then accumulates at paired centromeres where it may promote bi-orientation of homologous centromeres. We propose that, in addition to their roles as synaptonemal complex components, SYCP1 and SYCP3 act at the centromeres to promote the establishment and/or maintenance of centromere pairing and, by doing so, improve the segregation fidelity of mammalian meiotic chromosomes. 相似文献
11.
Bernhard Welsch 《Chromosoma》1973,43(1):19-74
Meiotic prophase in the spermatocytes ofPanorpa communis was studied. There is a proper sequence of meiotic stages in the testes. Therefore the temporal development of chromosome structure and the synaptonemal complex (SC) could be studied exactly. The structure and function of the SC are interpreted in a new model.—The chromosomes have a lambrush form from leptotene to diakinesis. At leptotene each chromatid produces an additional axis of basic protein and RNA. The axis becomes one of the lateral elements of the SC. At pachytene the DNA of the bivalents is separated into three regions: 1. Most of the DNA forms long loops outside the SC. 2. Smaller portions of the DNA filaments are twisted around the lateral elements of the SC. 3. Short DNA loops (called pairing loops) extend into the pairing space. InPanorpa the SC is composed of two lateral elements (chromosome axes), which are connected by equally spaced transverse filaments, a ladder-like central element in the middle of the pairing space and, on each side of the pairing space parallel to the lateral elements, two RNA containing strands. These are regarded as connected RNA copies of the pairing loops and are responsible for the exact pairing of homologous chromosome segments. At diplotene the axes of the sister chromatids separate to form “double complexes” with four lateral elements. The double complexes of the oocytes contain only transverse filaments between the axes of the homologous chromatids. After a short time they disappear again and the homologues separate to form the chiasmatic bivalents. In the spermatocytes all four chromatid axes are connected by transverse filaments. The pairing complex persists until diakinesis, thereby causing the suppression of the diplotene stage in the light microscope. This may be the only reason for the achiasmatic meiosis in the spermatocytes ofPanorpa. 相似文献
12.
Zip1-induced changes in synaptonemal complex structure and polycomplex assembly 总被引:19,自引:4,他引:15
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《The Journal of cell biology》1995,128(4):455-466
The yeast Zip1 protein is a component of the synaptonemal complex (SC), which is an elaborate macromolecular structure found along the lengths of chromosomes during meiosis. Mutations that increase the length of the predicted coiled coil region of the Zip1 protein show that Zip1 influences the width of the SC. Overexpression of the ZIP1 gene results in the formation of two distinct types of higher order structures that are found in the nucleus, but not associated with chromatin. One of these structures resembles the polycomplexes that have been observed in many organisms and are thought to be aggregates of SC components. The second type of structure, which we have termed "networks," does not resemble any previously identified SC-related structure. Assembly of both polycomplexes and networks can occur independently of the Hop1 or Red1 protein, which are thought to be SC components. Our results demonstrate that Zip1 is a structural component of the central region of the SC. More specifically, we speculate that Zip1 is a component of the transverse filaments that lie perpendicular to the long axis of the complex. 相似文献
13.
14.
Meiotic chromosome structure and function are described in the plant-parasitic nematode Heterodera betulae. Twelve synaptonemal complexes (SCs) were reconstructed from pachytene nuclei; therefore, n=12 is predicted for this species. Morphologically distinct sex chromosomes were not observed. Only one end of the SC is attached to the nuclear envelope, and there is no bouquet arrangement at pachytene. The structure of the SC in this meiotic parthenogenetic nematode was different than in other nematodes that reproduce via amphimixis; a striated central element with transverse filaments was not observed. Multiple SCs, or polycomplexes, were present in the nucleus. Recombination nodules were not observed. The centrioles were comprised of nine doublet microtubules connected by a ring, which is a distinct modification from the typical nine triplet microtubules without any interconnecting structure. 相似文献
15.
The synaptonemal complex plays a key role in pairing of homologous chromosomes during meiosis. Its gross structure was already known by conventional electron microscopy, but only recently has it been possible to reveal the synaptonemal complex in three dimensions at higher resolution by electron microscope tomography. As the molecular analysis of meiosis is developing rapidly, a more thorough understanding of the principal organization of the synaptonemal complex is essential. 相似文献
16.
Annelise Fiil 《Chromosoma》1978,69(3):381-395
The synaptonemal complexes of the oocytes of the mosquito Culex pipiens quinquefasciatus have been reconstructed from serial sections. A diffuse structure, probably a chromocenter composed of centromeric heterochromatin, was present during pachytene. As no synaptonemal complexes were visible inside the chromocenter the continuity of the 2 arms of a bivalent was lost. The telomeric ends were clustered in a small area of the nuclear membrane in a bouquet arrangement; they were associated in pairs, and sometimes joined through a special structure. One pair was composed of the 2 telomeres of the shortest bivalent and a ring configuration was thus formed. The other 2 chromosomes may form one or two rings. During a short transitional stage, after the disappearence of the synaptonemal complexes, several thousand annuli, 1200–1500 A in diameter, were present in the nuclei. The annuli disappeared as material originating mainly from the transverse filaments of the synaptonemal complexes formed a capsule around the chromosomes during diplotene. 相似文献
17.
Ewelina Bolcun-Filas Robert Speed Mary Taggart Corinne Grey Bernard de Massy Ricardo Benavente Howard J. Cooke 《PLoS genetics》2009,5(2)
In mammals, the synaptonemal complex is a structure required to complete crossover recombination. Although suggested by cytological work, in vivo links between the structural proteins of the synaptonemal complex and the proteins of the recombination process have not previously been made. The central element of the synaptonemal complex is traversed by DNA at sites of recombination and presents a logical place to look for interactions between these components. There are four known central element proteins, three of which have previously been mutated. Here, we complete the set by creating a null mutation in the Syce1 gene in mouse. The resulting disruption of synapsis in these animals has allowed us to demonstrate a biochemical interaction between the structural protein SYCE2 and the repair protein RAD51. In normal meiosis, this interaction may be responsible for promoting homologous synapsis from sites of recombination. 相似文献
18.
From data on the molecular organization of transverse filament proteins of the synaptonemal complex (SC)--Zip1 in yeast and SCP1 in mammals--and on the width of the central SC space in these organisms and in Drosophila, the putative molecular structure and size of a transverse filament protein of the SC in Drosophila has been inferred. Using genetic and molecular databases and software from the Internet, we carried out in silico screening for a candidate gene for the Drosophila transverse filament protein. The search in the 250-bp region overlapping the locus of this gene (sections 88E-89B) and containing 78 predicted genes has revealed only one gene, CG17604, whose protein meets all requirements for the transverse filament protein of the SC. It was suggested that gene CG17604 is gene c(3)G. In this case, gene c(3)G must be localized in section 89A7-8 of the cytological map of Drosophila melanogaster. 相似文献
19.
More detailed observations of the synaptonemal complex (SC) in asynaptic maize plants have been faciliated by superior silver-staining procedures. These suggest that central region components of the SC are strongly implicated as defective in asynaptic. Apparently homologous axial elements tend to follow roughly parallel courses within the nucleus at pachytene, in some short segments apparently synapsed and in others at wider separation than normal synapsis yet close enough to allow observation of thin central element segments and also occasional thin transverse element-type structures. This kind of transverse filament may be weakened and severely stretched yet associated with both axial elements. Small nodules, similar to recombination nodules, appear at corresponding positions in widely separated axial elements. Key words : synaptonemal complex, central element, transverse filament, recombination nodule. 相似文献
20.
The synaptonemal complex is a meiosis-specific structure essential for synapsis of homologous chromosomes. The synaptonemal complex protein 1 (SCP1) is a major constituent of the transversal filament, a fibrous structure that connects the central element of the synaptonemal complex with the two lateral elements. The SCP1 protein forms filamentous dimers with the two molecules that have the same polarity, with the C-termini being anchored in the lateral elements and the N-termini reaching into the central element. We investigated whether the SCP1 protein can take part in the formation of higher order protein structures by expressing it in a heterologous system. We find that expression of SCP1 in Swiss-3T3 fibroblast cells results in the formation of large protein structures. These protein structures resemble a higher order protein structure produced by overexpression of a yeast transversal filament protein in meiotic cells. Our results show that SCP1 is a structural protein and that it most likely is directly involved in the assembly of the synaptonemal complex. 相似文献