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"Davies, Owen"
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A supernatural war : magic, divination, and faith during the First World War
It was a commonly expressed view during the First World War that the conflict had seen a major revival of 'superstitious' beliefs and practices. Churches expressed concerns about the wearing of talismans and amulets, the international press paid considerable interest to the pronouncements of astrologers and prophets, and the authorities in several countries periodically clamped down on fortune tellers and mediums due to concerns over their effect on public morale. Out on the battlefields, soldiers of all nations sought to protect themselves through magical and religious rituals, and, on the home front, people sought out psychics and occult practitioners for news of the fate of their distant loved ones or communication with their spirits. Even away from concerns about the war, suspected witches continued to be abused and people continued to resort to magic and magical practitioners for personal protection, love, and success.
Book
BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode
BRCA2 is essential for DNA repair by homologous recombination in mitosis and meiosis. It interacts with recombinases RAD51 and DMC1 to facilitate the formation of nucleoprotein filaments on resected DNA ends that catalyse recombination-mediated repair. BRCA2’s BRC repeats bind and disrupt RAD51 and DMC1 filaments, whereas its PhePP motifs bind recombinases and stabilise their nucleoprotein filaments. However, the mechanism of filament stabilisation has hitherto remained unknown. Here, we report the crystal structure of a BRCA2-DMC1 complex, revealing how core interaction sites of PhePP motifs bind to recombinases. The interaction mode is conserved for RAD51 and DMC1, which selectively bind to BRCA2’s two distinct PhePP motifs via subtly divergent binding pockets. PhePP motif sequences surrounding their core interaction sites protect nucleoprotein filaments from BRC-mediated disruption. Hence, we report the structural basis of how BRCA2’s PhePP motifs stabilise RAD51 and DMC1 nucleoprotein filaments for their essential roles in mitotic and meiotic recombination.
This study presents the crystal structure of a BRCA2-DMC1 complex revealing how BRCA2’s PhePP motifs stabilise RAD51 and DMC1 nucleoprotein filaments during DNA double-strand break repair by mitotic and meiotic recombination.
Journal Article
Blockbusters and the ancient world : allegory and warfare in contemporary Hollywood
\"Following the release of Ridley Scott's Gladiator in 2000 the ancient world epic has experienced a revival in studio and audience interest. Building on existing scholarship on the Cold War epics of the 1950s-60s, including Ben-Hur, Spartacus and The Robe, this original study explores the current cycle of ancient world epics in cinema within the social and political climate created by September 11th 2001. Examining films produced against the backdrop of the War on Terror and subsequent invasions of Iraq and Afghanistan, this book assesses the relationship between mainstream cinema and American society through depictions of the ancient world, conflict and faith. Davies explores how these films evoke depictions of WWII, the Vietnam War and the Western in portraying warfare in the ancient world, as well discussing the influence of genre hybridisation, narration and reception theory. He questions the extent to which ancient world epics utilise allegory, analogy and allusion to parallel past and present in an industry often dictated by market forces. Featuring analysis of Alexander, Troy, 300, Centurion, The Eagle, The Passion of the Christ and more, this book offers new insight on the continued evolution of the ancient world epic in cinema\"-- Provided by publisher.
Book
السحر : مقدمة قصيرة جدا
لطالما جذب مفهوم السحر وممارسته اهتمام علماء النفس والاجتماع، وعلماء اللاهوت والأنثروبولوجيا، والفنانين، والمؤرخين. وحتى اليوم، لا تزال قضية السحر تسيطر على الخيال الشعبي. لكن لا يمكن أن نعتبر السحر جزءا من الماضي، أو ننبذه بوصفه نتيجة مباشرة للجهل، أو نصنفه على أنه مرحلة تطورية من مراحل الفكر الإنساني، على الأقل ليس من المنظور الثقافي. نعم، لقد قوض العلم أساس السحر بوصفه تفسيرا للعمليات الطبيعية، لكنه لا يستطيع التغاضي عنه؛ فالسحر سيظل دائما بديلا قائما.
Book
Crossover recombination and synapsis are linked by adjacent regions within the N terminus of the Zip1 synaptonemal complex protein
Accurate chromosome segregation during meiosis relies on the prior establishment of at least one crossover recombination event between homologous chromosomes. Most meiotic recombination intermediates that give rise to interhomolog crossovers are embedded within a hallmark chromosomal structure called the synaptonemal complex (SC), but the mechanisms that coordinate the processes of SC assembly (synapsis) and crossover recombination remain poorly understood. Among known structural components of the budding yeast SC, the Zip1 protein is unique for its independent role in promoting crossover recombination; Zip1 is specifically required for the large subset of crossovers that also rely on the meiosis-specific MutSγ complex. Here we report that adjacent regions within Zip1's N terminus encompass its crossover and synapsis functions. We previously showed that deletion of Zip1 residues 21-163 abolishes tripartite SC assembly and prevents robust SUMOylation of the SC central element component, Ecm11, but allows excess MutSγ crossover recombination. We find the reciprocal phenotype when Zip1 residues 2-9 or 10-14 are deleted; in these mutants SC assembles and Ecm11 is hyperSUMOylated, but MutSγ crossovers are strongly diminished. Interestingly, Zip1 residues 2-9 or 2-14 are required for the normal localization of Zip3, a putative E3 SUMO ligase and pro-MutSγ crossover factor, to Zip1 polycomplex structures and to recombination initiation sites. By contrast, deletion of Zip1 residues 15-20 does not detectably prevent Zip3's localization at Zip1 polycomplex and supports some MutSγ crossing over but prevents normal SC assembly and Ecm11 SUMOylation. Our results highlight distinct N terminal regions that are differentially critical for Zip1's roles in crossing over and SC assembly; we speculate that the adjacency of these regions enables Zip1 to serve as a liaison, facilitating crosstalk between the two processes by bringing crossover recombination and synapsis factors within close proximity of one another.
Journal Article
South American independence : gender, politics, text
The struggles for independence in Latin America during the first half of the nineteenth century were accompanied by a wide-ranging debate about political rights, nationality and citizenship. In South American Independence, Catherine Davies, Claire Brewster and Hilary Owen investigate the neglected role of gender in that discussion. Examining women writers from Brazil, Argentina, Chile, Peru, and Colombia, the book traces the contradictions inherent in revolutionary movements that, while arguing for the rights of all, remained ambivalent, at best, about the place of women. Through studies of both published and unpublished writings, South American Independence reveals the complex role of women in shaping the vexed ideologies of independence. -- Publisher description.
Book
MEILB2-BRME1 forms a V-shaped DNA clamp upon BRCA2-binding in meiotic recombination
DNA double-strand break repair by homologous recombination has a specialised role in meiosis by generating crossovers that enable the formation of haploid germ cells. This requires meiosis-specific MEILB2-BRME1, which interacts with BRCA2 to facilitate loading of recombinases onto resected DNA ends. Here, we report the crystal structure of the MEILB2-BRME1 2:2 core complex, revealing a parallel four-helical assembly that recruits BRME1 to meiotic double-strand breaks in vivo. It forms an N-terminal β-cap that binds to DNA, and a MEILB2 coiled-coil that bridges to C-terminal ARM domains. Upon BRCA2-binding, MEILB2-BRME1 2:2 complexes dimerize into a V-shaped 2:4:4 complex, with rod-like MEILB2-BRME1 components arranged at right-angles. The β-caps located at the tips of the MEILB2-BRME1 limbs are separated by 25 nm, allowing them to bridge between DNA molecules. Thus, we propose that BRCA2 induces MEILB2-BRME1 to function as a DNA clamp, connecting resected DNA ends or homologous chromosomes to facilitate meiotic recombination.
MEILB2-BRME1 is a BRCA2-binding complex that is required for meiotic recombination. Here, the authors report the structure and DNA-binding of MEILB2-BRME1, revealing how its BRCA2-induced dimerization forms a V-shaped assembly that may clamp together DNA molecules to facilitate recombination.
Journal Article
Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12
The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 μm) depends on its midline α-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building block and on assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fiber assembly. SYCE2-TEX12’s building blocks are 2:2 coiled coils that dimerize into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibers that intertwine within 40-nm bundled micrometer-long fibers that define the SC’s midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behavior typical of cytoskeletal proteins to provide an α-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes.
Crystallographic, electron microscopy and biophysical studies reveal how the synaptonemal complex component SYCE2-TEX12 undergoes self-assembly into fibrous supramolecular structures that mediate homologous chromosome synapsis in meiosis.
Journal Article
A molecular model for the role of SYCP3 in meiotic chromosome organisation
The synaptonemal complex (SC) is an evolutionarily-conserved protein assembly that holds together homologous chromosomes during prophase of the first meiotic division. Whilst essential for meiosis and fertility, the molecular structure of the SC has proved resistant to elucidation. The SC protein SYCP3 has a crucial but poorly understood role in establishing the architecture of the meiotic chromosome. Here we show that human SYCP3 forms a highly-elongated helical tetramer of 20 nm length. N-terminal sequences extending from each end of the rod-like structure bind double-stranded DNA, enabling SYCP3 to link distant sites along the sister chromatid. We further find that SYCP3 self-assembles into regular filamentous structures that resemble the known morphology of the SC lateral element. Together, our data form the basis for a model in which SYCP3 binding and assembly on meiotic chromosomes leads to their organisation into compact structures compatible with recombination and crossover formation. When a sperm cell and an egg cell unite, each contributes half of the genetic material needed for the fertilised egg to develop. This creates opportunities for new and beneficial genetic combinations to arise. To ensure that each new sperm or egg has half a set of chromosomes, reproductive cells undergo a special type of division called meiosis. During the early stages of meiosis, copies of each chromosome—one inherited from the mother, the other from the father—are paired up along the midline of the dividing cell. A protein complex known as the synaptonemal complex acts as a ‘zipper’, pulling the chromosomes in each pair closer together. The arms of the maternal chromosome and the paternal chromosome are so close that they sometimes cross over and swap a section of DNA. These crossovers perform two critical functions. First, they recombine the genetic information of a cell, so that offspring can benefit from new gene combinations. Second, they help to hold the chromosomes together at a key point of meiosis, reducing the chances that the wrong number of chromosomes ends up in a sperm or egg cell. The zipper structure is essential for meiosis. Disrupting its formation causes infertility and miscarriage in humans and mice, as well as chromosomal disorders like Down's syndrome. Scientists have known about this zipper structure and its importance since 1956, yet limited information is available about its shape and how it works. Syrjänen et al. used X-ray crystallography to take images of the part of the zipper structure that interacts with the chromosomes. These images, combined with the results of biochemical and biophysical experiments, show that rod-like structures on the zipper link together sites within each chromosome. This not only allows the paired chromosomes to be held together by the zipper, but also compacts them so it's easier for them to cross over and swap genetic information.
Journal Article