Context, Complexity and Contestation: Birmingham's Agreed Syllabuses for Religious Education since the 1970s

publication-status: AcceptedThis is an Author's Original Manuscript of an article whose final and definitive form, the Version of Record, has been published in the Journal of Beliefs and Values, September 2011. Available online at: http://www.tandfonline.com/ or DOI: 10.1080/13617672.2011.600823The present article offers an historical perspective on the 1975, 1995 and 2007 Birmingham Agreed Syllabuses for Religious Education. It draws upon historical evidence uncovered as part of ‘The hidden history of curriculum change in religious education in English schools, 1969–1979’ project, and curriculum history theories, especially David Labaree’s observations about the distance between the ‘rhetorical’ and ‘received’ curricula. We argue that, contrary to the existing historiography, curriculum change in religious education (RE) has been evolutionary not revolutionary. Multiple reasons are posited to explain this, not least among which is the capacity and agency of teachers. Furthermore, we argue that ongoing debates about the nature and purpose of RE, as exemplified in the Birmingham context, reflect the multiple expectations that religious educators and other stakeholders had, and continue to have, of the curriculum subject. These debates contribute to the inertia evident in the implementation of RE curriculum reforms. A consciousness of the history of RE enables curriculum contestations to be contextualised and understood, and, thereby, provides important insights which can be applied to ongoing and future debates and developments

Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin

A free-energy-based approach is used to describe the mechanism through which chaperonin-containing TCP-1 (CCT) folds the filament-forming cytoskeletal protein actin, which is one of its primary substrates. The experimental observations on the actin folding and unfolding pathways are collated and then re-examined from this perspective, allowing us to determine the position of the CCT intervention on the actin free-energy folding landscape. The essential role for CCT in actin folding is to provide a free-energy contribution from its ATP cycle, which drives actin to fold from a stable, trapped intermediate I3, to a less stable but now productive folding intermediate I2. We develop two hypothetical mechanisms for actin folding founded upon concepts established for the bacterial type I chaperonin GroEL and extend them to the much more complex CCT system of eukaryotes. A new model is presented in which CCT facilitates free-energy transfer through direct coupling of the nucleotide hydrolysis cycle to the phases of actin substrate maturation

Association of a Nonmuscle Myosin II with Axoplasmic Organelles

Association of motor proteins with organelles is required for the motors to mediate transport. Because axoplasmic organelles move on actin filaments, they must have associated actin-based motors, most likely members of the myosin superfamily. To gain a better understanding of the roles of myosins in the axon we used the giant axon of the squid, a powerful model for studies of axonal physiology. First, a ∼220 kDa protein was purified from squid optic lobe, using a biochemical protocol designed to isolate myosins. Peptide sequence analysis, followed by cloning and sequencing of the full-length cDNA, identified this ∼220 kDa protein as a nonmuscle myosin II. This myosin is also present in axoplasm, as determined by two independent criteria. First, RT-PCR using sequence-specific primers detected the transcript in the stellate ganglion, which contains the cell bodies that give rise to the giant axon. Second, Western blot analysis using nonmuscle myosin II isotype-specific antibodies detected a single ∼220 kDa band in axoplasm. Axoplasm was fractionated through a four-step sucrose gradient after 0.6 M KI treatment, which separates organelles from cytoskeletal components. Of the total nonmuscle myosin II in axoplasm, 43.2% copurified with organelles in the 15% sucrose fraction, while the remainder (56.8%) was soluble and found in the supernatant. This myosin decorates the cytoplasmic surface of 21% of the axoplasmic organelles, as demonstrated by immunogold electron-microscopy. Thus, nonmuscle myosin II is synthesized in the cell bodies of the giant axon, is present in the axon, and is associated with isolated axoplasmic organelles. Therefore, in addition to myosin V, this myosin is likely to be an axoplasmic organelle motor