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The loss of biodiversity through a rapidly changing climate means humans can no longer assume their longevity on Earth; a crisis that has prompted a wave of literary imaginings. This thesis will examine two eco-narratives through an ecocritical and narratological framework: Maja Lunde’s The History of Bees (2015) and Richard Powers’ The Overstory (2018), which envision starkly different ethical approaches and corollaries to the question of human response to ecological crisis. My thesis argues that these novels perform crucial cultural work in destabilising myopic perspectives on human and environmental paradigms. Anthropocentrism is a pivotal force shaping humanity’s hierarchical relationship with the environment and thus shaping attitudes towards climate change. Through examining narrative techniques of worldbuilding, focalisation of the human and more-than-human, and temporal movement, my thesis explores how Lunde and Powers repurpose key tenets of the novel form in order to encapsulate human and ecological experiences. Both novels thus demonstrate literature’s capacity to facilitate holistic rather than anthropocentric depictions of nature and of time. Furthermore, the novels operate as instances of literary provocation in a context of climate change, seen in Lunde’s attempts to inspire human and environmental symbiosis and in Powers’ fervent acknowledgement of ecological endurance and human insignificance. In the juxtaposition of two modern novels that address three crucial ecocritical themes, I will expose diverse portrayals of humanity’s relationship with the environment. The comparative analysis of these novels crystallises the value of ecological literature in offering diverse depictions of human relationships with the more-than-human world. My thesis thus critically contributes to ecocritical scholarship by exploring literature’s intervention in climate change discourse through analysing Lunde’s and Powers’ imaginative capacities to pose ethical alternatives to engaging with, and responding to, the urgency of climate change.

The actin cytoskeleton is a large, complex, dynamic network that is responsible for a myriad of cellular processes, including, polarity, endocytosis, motility, cytokinesis, and force response. Distinct filamentous actin (F-actin) networks assemble from one crowded cytoplasm. The ability to build several F-actin networks simultaneously with distinct architectures, dynamics, location, and timing is a topic that has drawn a lot of interest. Each of these F-actin networks associate with a set of actin binding proteins (ABPs). How ABPs sort and and contribute to the properties of the F-actin networks is a big question in cell biology. Our lab has done extensive research on different ABPs and the roles in corresponding F-actin networks. Our lab does use fission yeast for cell level analysis of F-actin networks. However, a large part of our research is minimal reconstitution of F-actin networks in vitro to directly investigate actin binding proteins. My contribution to the following projects is the minimal reconstitution biochemistry experiments. A relatively new topic in our lab is mechanosensitive ABPs, and I reconstitute actomyosin networks to study mechanosensitive ABP localization. LIM domain proteins have been studied by previous labs. There are over 70 mammalian LIM domain proteins, and several have been shown to associate with the actin cytoskeleton. In fact, many of them are involved in mechanotransduction pathways and associate with the F-actin networks in a force-dependent manner. Here, we studied the mechanism of mechanosensitive LIM domain protein recruitment with both in vivo assays and in vitro reconstitution assays. LIM domain proteins associate with force responsive F-actin networks: focal adhesions, adhesion junctions, stress fibers, and contractile ring. The LIM domain containing region (LCR) is essential for localization, and the LCR is hypothesized to bind directly to a force induced conformation of F-actin. Our lab and the Alushin lab made progress in understanding the LIM domain mechanosensitive mechanism, but there is still a lot left to be learned. Another ABP discussed here is Arp2/3 complex. Arp2/3 complex is a seven component protein that binds to actin filaments and nucleates branches. Arp2/3 complex networks are important for force generation, like the leading edge of motile cells or the endocytic patches. Arp2/3 complex has been studied extensively by many labs. However, the seven component structure has made fluorescent labeling difficult. We recently labeled the fission yeast Arp2/3 complex and have successfully visualized Arps/3 complex at the branch sites. We can now study the Arp2/3 complex-mediated branch formation pathway in greater detail and better understand the mechanism involved.

The global COVID-19 pandemic has created an urgent demand for accurate rapid point of care diagnostic tests. Antigen-based assays are suitably inexpensive and can be rapidly mass-produced, but sufficiently accurate performance requires highly-optimized antibodies and assay conditions. An automated liquid handling system, customized to handle lateral flow immunoassay (LFA) arrays, was used for high-throughput antibody screening of anti-nucleocapsid antibodies that will perform optimally on an LFA. Six hundred seventy-three anti-nucleocapsid antibody pairs were tested as both capture and detection reagents with the goal of finding those pairs that have the greatest affinity for unique epitopes of the nucleocapsid protein of SARS-CoV-2 while also performing optimally in an LFA format. In contrast to traditional antibody screening methods (e.g. ELISA, bio-layer interferometry), the methods described here integrate real-time LFA reaction kinetics and binding directly on nitrocellulose. We have identified several candidate antibody pairs that are suitable for further development of an LFA for SARS-CoV-2.