91 research outputs found
James Cooper and the Scoto-Catholic Party : tractarian reform in the Church of Scotland, 1882 - 1918
No full textIn Scotland, no less than in England, the late Victorian era was one of transition. Industrialisation and urbanisation created new social problems, while other forces - most importantly the railway - worked to undermine the national comprehensiveness of Scotland. Even Scottish religion, until now protected both by distance and the different polity entertained, fell under the sway of English influence.
This thesis considers one particular aspect of English influence upon the Church of Scotland - Tractarianism. There is clear evidence to prove that in liturgical and architectural expression, in church furnishings and arrangement, in ritual and in doctrine, and even in the development of a library of historical research, there was manifest by some a deliberate attempt to reform the Church of Scotland through a thorough-going application of Tractarian definitions, ideals, and symbolic expressions.
In particular the thesis investigates the personal influence of the Reverend Professor James Cooper in this endeavour, for he was one of the principal figures in changing the face of the Kirk. He was a medievalist, tinctured with Jacobitism. Although there were some in the Church with more profound learning, and others with a broader vision of the social and ecclesiastical requirements of the new age, Cooper combined within himself many of the aims, the ideals, and the foibles commonly associated with Victorians. As the representative spokesman for the Scoto-Catholic party, he held a unique place in the life of the Scottish Church, for the scoto-Catholics, though always few in number, were not without significant influence. It was they in particular who perpetrated the “Tractarian" reform in the Church of Scotland.
In the introduction the historical background to the Scottish Church in 1882 is sketched. Part I provides a background survey of the Oxford Movement in England and Scotland. Part II considers the Broad Church attempt at reform, and the liturgical developments associated with the Church Service Society. Part III deals with the emergence of Scoto-Catholicism, and Part IV with Ecclesiological and Ritualistic movements. Part V looks at the attempt to defend and advance Catholic doctrine - the programme of the Scottish Church Society, and also traces Cooper's influence on the "Articles Declaratory” of the constitution of the Church of Scotland. Part VI investigates the attempt to defend and advance Catholic authority in the Scottish Church through a restatement of the Tractarian doctrine of Apostolic
Succession. Of necessity it also considers the matters of ordination and "valid Orders". It is shown that by means of a "historiological mythos" the Scoto-Catholic position in this, as in other matters, was advanced. There are several appendices, the first of which traces a connection between the Catholic Apostolic Church - which itself was not without significant liturgical and doctrinal effect upon the Church of Scotland - and the Oxford Movement
Structural insights into the autoregulation and cooperativity of the human transcription factor Ets-2
No full textEts-2, like its closely related homologue Ets-1, is a member of the Ets family of DNA binding transcription factors. Both proteins are subject to multiple levels of regulation of their DNA binding and transactivation properties. One such regulatory mechanism is the presence of an autoinhibitory module, which in Ets-1 allosterically inhibits the DNA binding activity. This inhibition can be relieved by interaction with protein partners or cooperative binding to closely separated Ets binding sites in a palindromic arrangement. In this study we describe the 2.5 Å resolution crystal structure of a DNA complex of the Ets-2 Ets domain. The Ets domain crystallized with two distinct species in the asymmetric unit, which closely resemble the autoinhibited and DNA bound forms of Ets-1. This discovery prompted us to re-evaluate the current model for the autoinhibitory mechanism and the structural basis for cooperative DNA binding. In contrast to Ets-1, in which the autoinhibition is caused by a combination of allosteric and steric mechanisms, we were unable to find clear evidence for the allosteric mechanism in Ets-2. We also demonstrated two possibly distinct types of cooperative binding to substrates with Ets binding motifs separated by four and six base pairs and suggest possible molecular mechanisms for this behavior
Correction to: A multi-center analysis of adverse events among two thousand, three hundred and seventy two adult patients undergoing adult autologous stem cell therapy for orthopaedic conditions
No full textThe published online version contains mistake in Acknowledgment Section. The author name "Steve Gorin, M.D." should have been "Steven Gorin, D.O, M.S.Ed."
Structures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: Determinants of DNA Binding and Redox Regulation by Disulfide Bond Formation.
No full textEts transcription factors, which share the conserved Ets DNA-binding domain, number nearly 30 members in humans and are particularly involved in developmental processes. Their deregulation following changes in expression, transcriptional activity, or by chromosomal translocation plays a critical role in carcinogenesis. Ets DNA binding, selectivity, and regulation have been extensively studied; however, questions still arise regarding binding specificity outside the core GGA recognition sequence and the mode of action of Ets post-translational modifications. Here, we report the crystal structures of Etv1, Etv4, Etv5, and Fev, alone and in complex with DNA. We identify previously unrecognized features of the protein-DNA interface. Interactions with the DNA backbone account for most of the binding affinity. We describe a highly coordinated network of water molecules acting in base selection upstream of the GGAA core and the structural features that may account for discrimination against methylated cytidine residues. Unexpectedly, all proteins crystallized as disulfide-linked dimers, exhibiting a novel interface (distant to the DNA recognition helix). Homodimers of Etv1, Etv4, and Etv5 could be reduced to monomers, leading to a 40-200-fold increase in DNA binding affinity. Hence, we present the first indication of a redox-dependent regulatory mechanism that may control the activity of this subset of oncogenic Ets transcription factors
N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools
No full textSoluble protein expression is a key requirement for biochemical and structural biology approaches to study biological systems in vitro. Production of sufficient quantities may not always be achievable if proteins are poorly soluble which is frequently determined by physico-chemical parameters such as intrinsic disorder. It is well known that discrete protein domains often have a greater likelihood of high-level soluble expression and crystallizability. Determination of such protein domain boundaries can be challenging for novel proteins. Here, we outline the application of bioinformatics tools to facilitate the prediction of potential protein domain boundaries, which can then be used in designing expression construct boundaries for parallelized screening in a range of heterologous expression systems
Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway
No full textDNA polymerase theta (Polθ) has been identified as a crucial alternative non-homologous end-joining factor in mammalian cells. Polθ is upregulated in a range of cancer cell types defective in homologous recombination, and knockdown has been shown to inhibit cell survival in a subset of these, making it an attractive target for cancer treatment. We present crystal structures of the helicase domain of human Polθ in the presence and absence of bound nucleotides, and a characterization of its DNA-binding and DNA-stimulated ATPase activities. Comparisons with related helicases from the Hel308 family identify several unique features. Polθ exists as a tetramer both in the crystals and in solution. We propose a model for DNA binding to the Polθ helicase domain in the context of the Polθ tetramer, which suggests a role for the helicase domain in strand annealing of DNA templates for subsequent processing by the polymerase domain
Recent advances in the structural molecular biology of Ets transcription factors: interactions, interfaces and inhibition.
No full textThe Ets family of eukaryotic transcription factors is based around the conserved Ets DNA-binding domain. Although their DNA-binding selectivity is biochemically and structurally well characterized, structures of homodimeric and ternary complexes point to Ets domains functioning as versatile protein-interaction modules. In the present paper, we review the progress made over the last decade to elucidate the structural mechanisms involved in modulation of DNA binding and protein partner selection during dimerization. We see that Ets domains, although conserved around a core architecture, have evolved to utilize a variety of interaction surfaces and binding mechanisms, reflecting Ets domains as dynamic interfaces for both DNA and protein interaction. Furthermore, we discuss recent advances in drug development for inhibition of Ets factors, and the roles structural biology can play in their future
Development of biomechanical models that represent members of the South African National Defence Force
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