Circular Evolutions of Imaginative Maturation in Charlotte Brontë’s Jane Eyre and Villette

An exploration into the complex underpinnings of an evolving mind, Jane Eyre is both a literal and metacognitive inquiry into the implications of imagination. Principally dealing with the title character's stepwise assumption of identity, from a reticent orphan to a self-assured and socially empowered woman, Jane's is first and foremost a quest for love and community. However, underlying her linear search for the elusive domestic cornerstones of "family" and "home" is a relentless struggle between reality and imagination. Characterized by two consecutive arcs of imaginative maturation, Jane is presented first as an innocent, reveling immoderately in the novelty of uncharted conceptual possibility, then socialized into a form of self-imposed repression, and finally reintroduced into a subdued, cultivated imaginative landscape. Ultimately, although other Victorian intellects considered love to be the civilizing aspect unifying "intelligence and instinct," Jane Eyre asserts that imagination is yet another definitive inner governor that, able to traverse both extremes, must be similarly reconciled. As such, Jane's recursive travails through the spectrum of imaginative frenzy and suppression are transformed by her romantic indulgence. When requited, Jane and Mr. Rochester's love for one another combines the wish-fulfillment of romantic desires with the realism of a practicable union, thereby effectively distilling imagination into its more productive, governable, and expansive components. On the other hand, Lucy Snowe is a protagonist haunted by the incongruities between imagination and reason. Predisposed to thrive in a realm in which she is both arbitress and editor of these two, inherently contradictory, spheres, she chooses to craft a narrative in which she preferentially favors the real over the ideal, and excises any information that compromises her emotional anonymity, or her self-image as a fully prudent, circumspect, and proper Protestant lady. The account that results is likewise characterized, particularly in its beginnings, by a frustratingly scarce and occasionally incomplete tale that relies heavily upon accounts of the dramas of other characters rather than Lucy's own perspectives. As such, Lucy willfully manufactures the initial narrative so that she is a centrifugal player, interacting crucially with each supporting character, and utilizing the trajectories of their more central stories to reflectively reveal aspects of her own personality. As the story progresses, however, Lucy's imagination begins to increasingly collide with her carefully constructed reality. Her maturation during the course of the book is characterized by three distinct imaginative arcs. Each of these sequences is catalyzed by the intrusion of a particular emotional excess, the surfeit of which causes her to, however briefly, immoderately succumb to the lure of intemperate imagination. In an attempt to compensate, she subsequently reconstructs her psychological boundaries, undergoing a period of self-imposed normativity in which she either symbolically suppresses her desires, or replaces them with domestic pursuits. However, as the sources of her distress begin to increasingly reflect on the incongruities between her expanding desires and the limited social, romantic, and emotional requirements of her gender, she is forced to use the mitigating platform of the arts to safely explore alternatives to conventional womanhood. Ultimately, Lucy uses the guise of performativity to safely fuse the realms of realism and imagination, and manufacture a liminal space in which she can safely reconcile social stricture, independent ambition, and romantic fulfillment.No embargoAcademic Major: Englis

The Effect of EF-P on tRNA Ribosomal P-site Binding

A significant amount of research has been dedicated to characterizing how EF-P is intracellularly modified, as well as how it assists in stabilizing the ribosome during protein synthesis. Both of these functions involve the amino terminal domain of EF-P (also known as Domain I), which not only receives all modifications, but also makes critical positional contacts near the peptidyl transferase center and the aminoacyl acceptor stem of the initiator tRNA. (2) However, in 2009 Blaha, et al. published a structural analysis of EF-P that directed readers’ attention to additional contacts made between the Y180 and R183 residues of Domain III and the small ribosomal subunit. These residues were observed to interact with the A1339 and G1338 nucleotides in the 16S RNA of the 30S small ribosomal subunit of EF-P, which are thought to create a ‘gate’ between the P-site and E-site of the ribosome. They proposed that these interactions could help “prevent premature movement of the initiator tRNA to the E-site” or “enhance the gate [between the E- and the P-sites] and stabilize the fMet-tRNAifMet in the P-site.” (2) Likewise, this thesis is interested in the questions of whether these residues are essential for EF-P functionality in vivo, and whether they enhance EF-P’s function more than just by helping it interact with the ribosomal complex. The purpose of this project is to determine the effect of mutated EF-P residues on rates and success of ribosomal binding and interactions with the P-site tRNA. In order to address this question, we conducted site directed mutagenesis upon the Y180 and R183 residues of EF-P, and performed the following three assays: complementation assays to assess the growth phenotypes of the mutants; modification tests in which cell lysates were run on isoelectric focusing gels to determine whether the mutants were still aminoacylated with BLys; and, fMet puromycin reactivity assays to indirectly gauge the ability of the mutant EF-P to successfully bind to the ribosome.No embargoAcademic Major: Microbiolog

Oxidation of Cellular Amino Acid Pools Leads to Cytotoxic Mistranslation of the Genetic Code

Aminoacyl-tRNA synthetases use a variety of mechanisms to ensure fidelity of the genetic code and ultimately select the correct amino acids to be used in protein synthesis. The physiological necessity of these quality control mechanisms in different environments remains unclear, as the cost vs benefit of accurate protein synthesis is difficult to predict. We show that in Escherichia coli, a non-coded amino acid produced through oxidative damage is a significant threat to the accuracy of protein synthesis and must be cleared by phenylalanine-tRNA synthetase in order to prevent cellular toxicity caused by mis-synthesized proteins. These findings demonstrate how stress can lead to the accumulation of non-canonical amino acids that must be excluded from the proteome in order to maintain cellular viability

Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code.

Aminoacyl-tRNA synthetases use a variety of mechanisms to ensure fidelity of the genetic code and ultimately select the correct amino acids to be used in protein synthesis. The physiological necessity of these quality control mechanisms in different environments remains unclear, as the cost vs benefit of accurate protein synthesis is difficult to predict. We show that in Escherichia coli, a non-coded amino acid produced through oxidative damage is a significant threat to the accuracy of protein synthesis and must be cleared by phenylalanine-tRNA synthetase in order to prevent cellular toxicity caused by mis-synthesized proteins. These findings demonstrate how stress can lead to the accumulation of non-canonical amino acids that must be excluded from the proteome in order to maintain cellular viability

Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code.

Aminoacyl-tRNA synthetases use a variety of mechanisms to ensure fidelity of the genetic code and ultimately select the correct amino acids to be used in protein synthesis. The physiological necessity of these quality control mechanisms in different environments remains unclear, as the cost vs benefit of accurate protein synthesis is difficult to predict. We show that in Escherichia coli, a non-coded amino acid produced through oxidative damage is a significant threat to the accuracy of protein synthesis and must be cleared by phenylalanine-tRNA synthetase in order to prevent cellular toxicity caused by mis-synthesized proteins. These findings demonstrate how stress can lead to the accumulation of non-canonical amino acids that must be excluded from the proteome in order to maintain cellular viability

Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code.

Aminoacyl-tRNA synthetases use a variety of mechanisms to ensure fidelity of the genetic code and ultimately select the correct amino acids to be used in protein synthesis. The physiological necessity of these quality control mechanisms in different environments remains unclear, as the cost vs benefit of accurate protein synthesis is difficult to predict. We show that in Escherichia coli, a non-coded amino acid produced through oxidative damage is a significant threat to the accuracy of protein synthesis and must be cleared by phenylalanine-tRNA synthetase in order to prevent cellular toxicity caused by mis-synthesized proteins. These findings demonstrate how stress can lead to the accumulation of non-canonical amino acids that must be excluded from the proteome in order to maintain cellular viability