An ‘axe for the frozen sea’ : Estrin’s magic agential realism, insect thigmotaxis, and the problem with Kafka

This paper seeks to demonstrate how Marc Estrin’s Insect Dreams: the Half Life of Gregor Samsa constitutes the first piece of magic agential realist literature about insects. The term ‘magic agential realism’ has been coined from an observed coincidence in the literary commitments of Estrin’s novel to the literary genre of magic realism and the posthumanist assumptions it shares with the agential realism of Karen Barad. Given Kafka’s axiom that a literary work ought to function as an ‘axe for the frozen sea within us’. A further claim will be defended is the claim that Estrin’s Insect Dreams is the magic agential axe that shatters the frozen sea of liberal humanist representationalism within Kafka. In providing us with a book that affects us like a disaster and like a suicide (both of which are evoked and exceeded by the ever-more pressing concerns of posthumanism), I will demonstrate how Estrin both fulfils the literary criteria laid out by Kafka to Oskar Pollak and opens up the possibility of re-configuring ethics in order to account for insects through the observed phenomenon of thigmotaxis.peer-reviewe

Effects of mlc Gene Modulation on Acetate Accumulation in Escherichia Coli Culture

When Escherichia coli (E. coli) is grown in the presence of excess glucose, acetate is produced, oftentimes as an undesired by-product. Mlc is a global repressor for sugar transporters in E. coli, including glucose. This body of work examines the overexpression of Mlc via expression vectors in E. coli cultures under constitutive and inducible promoters. Sequence changes to the translational start codon and codon 52 of the mlc sequence inserted in the expression vectors were introduced. These changes were evaluated for their impact on glucose uptake rates, acetate production, and overall cell growth when Mlc was overexpressed in E. coli cultures in the presence of excess glucose. Furthermore, expression vectors carrying the mlc gene versions were co-transformed with a plasmid encoding for a therapeutic protein in order to study the impact of Mlc overexpression on the production of the therapeutic protein. Results showed varied levels of Mlc overexpression; however a correlation was drawn between increased Mlc expression and decreased acetate production as a result of slower glucose uptake into the cell. This characteristic resulted in improved cell growth in the form of higher density cultures. In addition to growing to higher cell densities, a 1.7-fold increase of therapeutic protein production was observed in cultures overexpressing Mlc, compared to the control

Novel form of adaptation in mouse retinal rods speeds recovery of phototransduction

Photoreceptors of the retina adapt to ambient light in a manner that allows them to detect changes in illumination over an enormous range of intensities. We have discovered a novel form of adaptation in mouse rods that persists long after the light has been extinguished and the rod's circulating dark current has returned. Electrophysiological recordings from individual rods showed that the time that a bright flash response remained in saturation was significantly shorter if the rod had been previously exposed to bright light. This persistent adaptation did not decrease the rate of rise of the response and therefore cannot be attributed to a decrease in the gain of transduction. Instead, this adaptation was accompanied by a marked speeding of the recovery of the response, suggesting that the step that rate-limits recovery had been accelerated. Experiments on knockout rods in which the identity of the rate-limiting step is known suggest that this adaptive acceleration results from a speeding of G protein/effector deactivation

Dinitrosyl formation as an intermediate stage of the reduction of NO in the presence of MoO_3

We present first-principles calculations in the framework of density-functional theory and the pseudopotential approach, aiming to model the intermediate stages of the reduction of NO in the presence of MoO$_3$(010). In particular, we study the formation of dinitrosyl, which proves to be an important intermediate stage in the catalytic reduction. We find that the replacement of an oxygen of MoO$_3$ by NO is energetically favorable, and that the system lowers further its energy by the formation of (NO)$_2$. Moreover, the geometry and charge distribution for the adsorbed dinitrosyl indicates a metal-oxide mediated coupling between the two nitrogen and the two oxygen atoms. We discuss the mechanisms for the dinitrosyl formation and the role of the oxide in the reaction.Comment: 6 pages, 4 figs, RevTeX. To be published in J. Chem. Phy

Co-expression of Gbeta 5 Enhances the Function of Two Ggamma Subunit-like Domain-containing Regulators of G Protein Signaling Proteins

Regulators of G protein signaling (RGS) stimulate the GTPase activity of G protein Galpha subunits and probably play additional roles. Some RGS proteins contain a Ggamma subunit-like (GGL) domain, which mediates a specific interaction with Gbeta 5. The role of such interactions in RGS function is unclear. RGS proteins can accelerate the kinetics of coupling of G protein-coupled receptors to G-protein-gated inwardly rectifying K+ (GIRK) channels. Therefore, we coupled m2-muscarinic acetylcholine receptors to GIRK channels in Xenopus oocytes to evaluate the effect of Gbeta 5 on RGS function. Co-expression of either RGS7 or RGS9 modestly accelerated GIRK channel kinetics. When Gbeta 5 was co-expressed with either RGS7 or RGS9, the acceleration of GIRK channel kinetics was strongly increased over that produced by RGS7 or RGS9 alone. RGS function was not enhanced by co-expression of Gbeta 1, and co-expression of Gbeta 5 alone had no effect on GIRK channel kinetics. Gbeta 5 did not modulate the function either of RGS4, an RGS protein that lacks a GGL domain, or of a functional RGS7 construct in which the GGL domain was omitted. Enhancement of RGS7 function by Gbeta 5 was not a consequence of an increase in the amount of plasma membrane or cytosolic RGS7 protein

Light-Dependent Translocation of Arrestin in the Absence of Rhodopsin Phosphorylation and Transducin Signaling

Visual arrestin plays a crucial role in the termination of the light response in vertebrate photoreceptors by binding selectively to light-activated, phosphorylated rhodopsin. Arrestin localizes predominantly to the inner segments and perinuclear region of dark-adapted rod photoreceptors, whereas light induces redistribution of arrestin to the rod outer segments. The mechanism by which arrestin redistributes in response to light is not known, but it is thought to be associated with the ability of arrestin to bind photolyzed, phosphorylated rhodopsin in the outer segment. In this study, we show that light-driven translocation of arrestin is unaffected in two different mouse models in which rhodopsin phosphorylation is lacking. We further show that arrestin movement is initiated by rhodopsin but does not require transducin signaling. These results exclude passive diffusion and point toward active transport as the mechanism for light-dependent arrestin movement in rod photoreceptor cells

Light-dependent translocation of arrestin in the absence of rhodopsin phophorylation and transducin signaling

Visual arrestin plays a crucial role in the termination of the light response in vertebrate photoreceptors by binding selectively to light-activated, phosphorylated rhodopsin. Arrestin localizes predominantly to the inner segments and perinuclear region of dark-adapted rod photoreceptors, whereas light induces redistribution of arrestin to the rod outer segments. The mechanism by which arrestin redistributes in response to light is not known, but it is thought to be associated with the ability of arrestin to bind photolyzed, phosphorylated rhodopsin in the outer segment. In this study, we show that light-driven translocation of arrestin is unaffected in two different mouse models in which rhodopsin phosphorylation is lacking. We further show that arrestin movement is initiated by rhodopsin but does not require transducin signaling. These results exclude passive diffusion and point toward active transport as the mechanism for light-dependent arrestin movement in rod photoreceptor cells

Modules in the photoreceptor RGS9-1•Gβ5L GTPase-accelerating protein complex control effector coupling, GTPase acceleration, protein folding, and stability

RGS (regulators of G protein signaling proteins regulate G protein signaling by accelerating GTP hydrolysis, but little is known about regulation of GTPase-accelerating protein (GAP) activities or roles of domains and subunits outside the catalytic cores. RGS9-1 is the GAP required for rapid recovery of light responses in vertebrate photoreceptors and the only mammalian RGS protein with a defined physiological function. It belongs to an RGS subfamily whose members have multiple domains, including G gamma -like domains that bind G(beta5) proteins. Members of this subfamily play important roles in neuronal signaling, Within the GAP complex organized around the RGS domain of RGS9-1, we have identified a functional role for the G gamma -like-G(beta 5L) complex in regulation of GAP activity by an effector subunit, cGMP phosphodiesterase gamma and in protein folding and stability of RGS9-1, The C-terminal domain of RGS9-1 also plays a major role in conferring effector stimulation. The sequence of the RGS domain determines whether the sign of the effector effect will be positive or negative. These roles were observed in, vitro using full-length proteins or fragments for RGS9-1, RGS7, G(beta 5S), and G(beta 5s), The dependence of RGS9-1 on Gp, co-expression for folding, stability, and function has been confirmed in vivo using transgenic Xenopus laevis, These results reveal how multiple domains and regulatory polypeptides work together to fine tune G(t alpha) inactivation