Student teaching is a cornerstone of teacher preparation, yet it remains one of the most difficult experiences to understand. Calls for an ecological approach to research on student teaching prompted this study in which the experience is examined from the perspective of the three key triad members. Using activity theory, this study explores how their interactions in specific contexts shaped opportunities for student teachers to learn to teach language arts. The findings reveal that all members of the triad were simultaneously operating in multiple settings and facing competing demands that shaped their actions and stances. Consequently, there were numerous instances of lost opportunities for student teachers to learn to teach, including sparse feedback on teaching subject matter and few links to methods courses, plus limited opportunities to develop identities as teachers. The structures that frame student teaching and its participants have deep roots in the cultures of universities and schools that must be considered if student teaching is to maximize its potential.
This is an author-produced, peer-reviewed version of this article. The final, definitive version of this document can be found online at Journal of Teacher Education, published by SAGE. Copyright restrictions may apply.
Protein synthesis and degradation determine the cellular levels of proteins, and their control hence enables organisms to respond to environmental change. Experimentally, these are little known proteome parameters; however, recently, SILAC-based mass spectrometry studies have begun to quantify turnover in the proteomes of cell lines, yeast, and animals. Here, we present a proteome-scale method to quantify turnover and calculate synthesis and degradation rate constants of individual proteins in autotrophic organisms such as algae and plants. The workflow is based on the automated analysis of partial stable isotope incorporation with (15)N. We applied it in a study of the unicellular pico-alga Ostreococcus tauri and observed high relative turnover in chloroplast-encoded ATPases (0.42-0.58% h(-1)), core photosystem II proteins (0.34-0.51% h(-1)), and RbcL (0.47% h(-1)), while nuclear-encoded RbcS2 is more stable (0.23% h(-1)). Mitochondrial targeted ATPases (0.14-0.16% h(-1)), photosystem antennae (0.09-0.14% h(-1)), and histones (0.07-0.1% h(-1)) were comparatively stable. The calculation of degradation and synthesis rate constants k(deg) and k(syn) confirms RbcL as the bulk contributor to overall protein turnover. This study performed over 144 h of incorporation reveals dynamics of protein complex subunits as well as isoforms targeted to different organelles.
The Earth’s rotation has driven the evolution of cellular circadian clocks to facilitate anticipation of the solar cycle. Some evidence for timekeeping mechanism conserved from early unicellular life through to modern organisms was recently identified, but the components of this oscillator are currently unknown. Although very few clock components appear to be shared across higher species, Casein Kinase 1 (CK1) is known to affect timekeeping across metazoans and fungi, but has not previously been implicated in the circadian clock in the plant kingdom. We now show that modulation of CK1 function lengthens circadian rhythms in Ostreococcus tauri , a unicellular marine algal species at the base of the green lineage, separated from humans by ~1.5 billion years of evolution. CK1 contributes to timekeeping in a phase-dependent manner, indicating clock-mediated gating of CK1 activity. Label-free proteomic analyses upon overexpression as well as inhibition revealed CK1-responsive phosphorylation events on a set of target proteins, including highly conserved potentially clock-relevant cellular regulator proteins. These results have major implications for our understanding of cellular timekeeping and can inform future studies in any circadian organism.
Protein-protein binding and signaling pathways are important fields of biomedical science. Here we report simple optical methods for the determination of the equilibrium binding constant K d of proteinprotein interactions as well as quantitative studies of biochemical cascades. The techniques are based on steady-state and time-resolved fluorescence resonance energy transfer (FRET) between ECFP and Venus-YFP fused to proteins of the SUMO family. Using FRET has several advantages over conventional free-solution techniques such as isothermal titration calorimetry (ITC): Concentrations are determined accurately by absorbance, highly sensitive binding signals enable the analysis of small quantities, and assays are compatible with multi-well plate format. Most importantly, our FRET-based techniques enable us to measure the effect of other molecules on the binding of two proteins of interest, which is not straightforward with other approaches. These assays provide powerful tools for the study of competitive biochemical cascades and the extent to which drug candidates modify protein interactions.
The purpose of this longitudinal study was to learn how beginning elementary teachers understood and used curriculum materials for teaching reading, and how, in turn, these materials shaped teachers' instruction. We followed 4 teachers who worked in markedly different school situations and were provided a variety of curriculum materials, ranging from scripted reading programs to supplemental materials without teaching guides. Data were gathered through classroom observations, interviews, and curriculum artifacts over the teachers' first 3 years on the job. Our analysis suggested that curriculum materials interacted with teachers' knowledge of reading and reading instruction, and with the contexts in which they worked. As a result, curriculum materials both fostered and inhibited teachers' on-the-job learning. We found that the 2 teachers with weak knowledge or more restrictive materials and environments learned the least and were least able to adapt instruction to meet the needs of their students. The 2 teachers with stronger knowledge, access to multiple materials, and support for decision making regarding materials and instructional strategies learned the most and were most able to adapt instruction. Furthermore, early experiences with specific curriculum materials had effects 2 years later on these teachers' instructional practices. Implications for curriculum mandates, material selection, and professional development are discussed.
Mitochondrial dysfunction is putatively central to glioblastoma (GBM) pathophysiology but there has been no systematic analysis in GBM of the proteins which are integral to mitochondrial function. Alterations in proteins in mitochondrial enriched fractions from patients with GBM were defined with label-free liquid chromatography mass spectrometry. 256 mitochondrially-associated proteins were identified in mitochondrial enriched fractions and 117 of these mitochondrial proteins were markedly (fold-change ≥2) and significantly altered in GBM (p ≤ 0.05). Proteins associated with oxidative damage (including catalase, superoxide dismutase 2, peroxiredoxin 1 and peroxiredoxin 4) were increased in GBM. Protein–protein interaction analysis highlighted a reduction in multiple proteins coupled to energy metabolism (in particular respiratory chain proteins, including 23 complex-I proteins). Qualitative ultrastructural analysis in GBM with electron microscopy showed a notably higher prevalence of mitochondria with cristolysis in GBM. This study highlights the complex mitochondrial proteomic adjustments which occur in GBM pathophysiology.Electronic supplementary materialThe online version of this article (doi:10.1007/s11060-014-1430-5) contains supplementary material, which is available to authorized users.
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