A Restorative Theory of Criminal Justice

In this project, I defend a restorative theory of criminal justice. I argue that the response to criminal wrongdoing in a just society should take the form of an attempt to heal the damage done to the community resulting from crime. I argue that the moral responsibilities of wrongdoers as wrongdoers ought to provide the framework for how a just society should respond to crime. Following the work of R.A. Duff, I argue that wrongdoers incur second-order duties of moral recognition. Wrongdoers owe it to others to recognize their wrongdoing for what it is, i.e. wrongdoing, and to shoulder certain burdens in order to express their repentant recognition to others via a meaningful apology. In short, wrongdoers owe it to their victims and others in the community to make amends. What I will deny, however, is the now familiar claim in the restorative justice literature that restoring the normative relationships in the community damaged by criminal forms of wrongdoing requires retributive punishment. In my view, how we choose to express the judgement that wrongdoers are blameworthy should flow from an all things considered judgment that is neither reducible to the judgement that the wrongdoer is culpably responsible for wronging others, nor the judgement that the wrongdoer in some basic sense “deserves to suffer” (or “deserves punishment,” etc.).

Functional characterization of a Kar3/Vik1-like Kinesin-14 heterodimer from the filamentous multinucleate fungus Ashbya gossypii

Kinesins are motor proteins that convert chemical energy from ATP hydrolysis into mechanical energy used to generate force along microtubules, transporting organelles, vesicles, and proteins within the cell. Kar3 kinesins are microtubule minus-end-directed motors with pleiotropic functions in mating and mitosis of budding and fission yeast. In Saccharomyces cerevisiae, Kar3 is multifunctionalized by two non-catalytic companion proteins, Vik1 and Cik1. A Kar3-like kinesin and a single Vik1/Cik1 ortholog are also expressed by the filamentous fungus Ashbya gossypii, which exhibits different nuclear movement challenges and unique microtubule dynamics from its yeast relatives. We hypothesized that these differences in A. gossypii physiology could translate into interesting and novel differences in its versions of Kar3 and Vik1/Cik1. Presented here is a structural and functional analysis of recombinantly expressed and purified forms of these motor proteins. Compared to the previously published S. cerevisiae Kar3 motor domain structure (ScKar3MD), AgKar3MD displays differences in the conformation of the ATPase pocket. Perhaps it is not surprising then that we observed the maximal microtubule-stimulated ATPase rate (kcat) of AgKar3MD to be approximately 3-fold slower than ScKar3MD, and that the affinity of AgKar3MD for microtubules (Kd,MT) was lower than ScKar3MD. This may suggest that elements that compose the ATPase pocket and that participate in conformational changes required for efficient ATP hydrolysis or products release work differently for AgKar3 and ScKar3. There are also subtle structural differences in the disposition of the secondary structural elements in the small lobe (B1a, B1b, and B1c) at the edge of the motor domain of AgKar3 that may reflect the enhanced microtubule-depolymerization activity that we observed for this motor, or they could relate to its interactions with a different regulatory companion protein than its budding yeast counterpart. Although we were unable to gain experimentally determined high-resolution information of AgVik1, the results of Phyre2-based bioinformatics analyses may provide a structural explanation for the limited microtubule-binding activity we observed. These and other fundamental differences in AgKar3/Vik1 could explain divergent functionalities from the ScKar3/Vik1 and ScKar3/Cik1 motor assemblies.