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Studying C9orf72 dipeptide repeat polypeptide aggregation using an analytical ultracentrifuge equipped with fluorescence detection
No full textElemental: Denise Ferreira da Silva’s raw materialist justice
No full textDenise Ferreira da Silva’s recent work, Unpayable Debt, makes a provocative intervention into current debates over and struggles for global justice in the wake of colonialism and in view of contemporary neo-colonial forces of extractive violence. Ferreira da Silva argues that only the return of the total value of the land and labor of the formerly enslaved and colonized would suffice to repay the debt owed to them by the global economy. Yet, such a debt is both unlimited in space and unrestricted in time, since that stolen land and expropriated labor are the very materiality of the global economy, past and present. For Ferreira da Silva, only a truly “raw materialist” apprehension of the scope of this debt, one which appreciates its elemental and cosmic composition, can enable decolonial justice to be conceived or achieved. In this paper, after outlining the arguments of Unpayable Debt, I elaborate Ferreira da Silva’s sense of the elemental stakes of global justice, extending and elaborating her thought through a reading of the recent afro-futurist film Neptune Frost (2021)
Reproducibility may be the key idea students need to balance trust in evidence with healthy skepticism
No full textEnnodio di Pavia: Cultura, letteratura, stile fra V e VI secolo, ed. Fabio Gasti. [book review]
No full textDeciphering culturally-coded institutional responses to COVID-19 adversity and anti-Asian hate in higher education
No full textA Phosphopantetheinyl Transferase from Dictyobacter vulcani sp. W12 Expands the Combinatorial Biosynthetic Toolkit
No full textThe value of microbial natural product pathways extends beyond the chemicals they produce, as the enzymes they encode can be harnessed as biocatalysts. Microbial type II polyketide synthases (PKSs) are particularly noteworthy, as these enzyme assemblies produce complex polyaromatic pharmacophores. Combinatorial biosynthesis with type II PKSs has been described as a promising route for accessing never-before-seen bioactive molecules, but this potential is stymied in part by the lack of functionally compatible noncognate proteins across type II PKS systems. Acyl carrier proteins (ACPs) are central to this challenge, as they shuttle reactive intermediates and malonyl building blocks between the other type II PKS domains during biosynthesis. To perform this essential role within PKSs, ACPs must first be activated to their holo state via the phosphopantetheinyl transferase (PPTase)-catalyzed installation of a coenzyme A (CoA)-derived phosphopantetheine (Ppant) arm. The installation of the Ppant arm is critical to effectively study and strategically engineer type II PKSs, yet not all ACPs can be activated using conventional PPTases. Here, we report the discovery of a previously unexplored nonactinobacterial PPTase from Dictyobacter vulcani sp. W12 (vulcPPT). We explored its compatibility with both native and non-native ACPs, observing that vulcPPT activated all ACPs tested in this study, including a noncognate, nonactinobacterial ACP that was not readily activated by the prototypical broad substrate PPTases AcpS and Sfp. Strategic optimization of phosphopantetheinylation reaction conditions increased the apo to holo conversion catalyzed by vulcPPT. In addition to identifying a promising new PPTase that is easy to prepare and use, this work establishes a roadmap for further investigation of PPTase compatibility and increases access to functional synthase components for use in combinatorial biosynthesis