Screening Diversity: Women & Work in Twenty-First-Century Popular Culture

Screening Diversity: Women and Work in Twenty-first Century Popular Culture explores contemporary representations of diverse professional women on screen. Audiences are offered successful women with limited concerns for feminism, anti-racism, or economic justice. I introduce the term viewsers to describe a group of movie and television viewers in the context of the online review platform Internet Movie Database (IMDb) and the social media platforms Twitter and Facebook. Screening Diversity follows their engagement in a representative sample of professional women on film and television produced between 2007 and 2015. The sample includes the television shows, Scandal, Homeland, VEEP, Parks and Recreation, and The Good Wife, as well as the movies, Zero Dark Thirty, The Proposal, The Heat, The Other Woman, I Don’t Know How She Does It, and Temptation. Viewsers appreciated female characters like Olivia (Scandal), and Maya (Zero Dark Thiry) who treated their work as a quasi-religious moral imperative. Producers and viewsers shared the belief that unlimited time commitment and personal identification were vital components of professionalism. However, powerful women, like The Proposal’s Margaret and VEEP’s Selina, were often called bitches. Some viewsers embraced bitch-positive politics in recognition of the struggles of women in power. Women’s disproportionate responsibility for reproductive labor, often compromises their ability to live up to moral standards of work. Unlike producers, viewsers celebrated and valued that labor. However, texts that included serious consideration of women as workers were frequently labelled chick flicks or soap operas. The label suggested that women’s labor issues were not important enough that they could be a topic of quality television or prestigious film, which bolstered the idea that workplace equality for women is not a problem in which the general public is implicated. Emerging discussions of racial injustice on television offered hope that these formations are beginning to shift.

STRUCTURE AND FUNCTION OF THE GROUP III CHAPERONINS, A UNIQUE CLADE OF PROTEIN FOLDING NANOMACHINES

The survival and descent of cells is universally dependent on maintaining their proteins in a properly folded condition. It is widely accepted that the information for the folding of the nascent polypeptide chain into a native protein is encrypted in the amino acid sequence, and the Nobel Laureate Christian Anfinsen was the first to demonstrate that a protein could spontaneously refold after complete unfolding. However, it became clear that the observed folding rates for many proteins were much slower than rates estimated in vivo. This led to the recognition of required protein-protein interactions that promote proper folding. A unique group of proteins, the molecular chaperones, are responsible for maintaining protein homeostasis during normal growth as well as stress conditions. Chaperonins (CPNs) are ubiquitous and essential chaperones. They form ATP-dependent, hollow complexes that encapsulate polypeptides in two back-to-back stacked multisubunit rings, facilitating protein folding through highly cooperative allosteric articulation. CPNs are usually classified into Group I and Group II. Here, I report the characterization of a novel CPN belonging to a third Group, recently discovered in bacteria. Group III CPNs have close phylogenetic association to the Group II CPNs found in Archaea and Eukarya, and may be a relic of the Last Common Ancestor of the CPN family. The gene encoding the Group III CPN from Carboxydothermus hydrogenoformans and Candidatus Desulforudis audaxviator was cloned in E. coli and overexpressed in order to both characterize the protein and to demonstrate its ability to function as an ATPase chaperone. The opening and closing cycle of the Chy chaperonin was examined via site-directed mutations affecting the ATP binding site at R155. To relate the mutational analysis to the structure of the CPN, the crystal structure of both the AMP-PNP (an ATP analogue) and ADP bound forms were obtained in collaboration with Sun-Shin Cha in Seoul, South Korea. The ADP and ATP binding site substitutions resulted in frozen forms of the structures in open and closed conformations. From this, mutants were designed to validate hypotheses regarding key ATP interacting sites as well as important stabilizing interactions, and to observe the physical properties of the resulting complexes by calorimetry.