Serine Protease Autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and Function

Serine Protease Autotransporters of Enterobacteriaceae (SPATEs) constitute a large family of proteases secreted by Escherichia coli and Shigella. SPATEs exhibit two distinct proteolytic activities. First, a C-terminal catalytic site triggers an intra-molecular cleavage that releases the N-terminal portion of these proteins in the extracellular medium. Second, the secreted N-terminal domains of SPATEs are themselves proteases; each contains a canonical serine-protease catalytic site. Some of these secreted proteases are toxins, eliciting various effects on mammalian cells. Here, we discuss the biogenesis of SPATEs and their function as toxins

New Maternalisms

"A weekend of performance, performance-based video, artist talks, and community events exploring the materiality of motherhood. " -- p. [2] of the cove

Performing Motherhood: Artistic, Activist and Everyday Enactments

"Performing Motherhood explores relationships between performativity and the maternal. Highlighting mothers’ lived experiences, this collection examines mothers’ creativity and agency as they perform in everyday life: in mothering, in activism, and in the arts. Chapters contain theoretically grounded works that emerge from multiple disciplines and cross-disciplines and include first-person narratives, empirical studies, artistic representations, and performance pieces. This book focuses on motherwork, maternal agency, mothers’ multiple identities and marginalized maternal voices, and explores how these are performatively constituted, negotiated and affirmed." -- Publisher's website

3D imaging of the 58 kDa cell binding subunit of the Helicobacter pylori cytotoxin.

Pathogenic strains of Helicobacter pylori produce a potent exotoxin, VacA, which intoxicates gastric epithelial cells and leads to peptic ulcer. The toxin is released from the bacteria as a high molecular mass homo-oligomer of a 95 kDa polypeptide which undergoes specific proteolytic cleavage to 37 kDa and 58 kDa subunits. We have engineered a strain of H. pylori to delete the gene sequence coding for the 37 kDa subunit. The remaining 58 kDa subunit is expressed efficiently and exported as a soluble dimer that is non-toxic but binds target cells in a manner similar to the holotoxin. A 3D reconstruction of the molecule from electron micrographs of quick-freeze, deep-etched preparations reveals the contribution of each building block to the structure and permits the reconstruction of the oligomeric holotoxin starting from individual subunits. In this model P58 subunits are assembled in a ring structure with P37 subunits laying on the top. The data indicate that the 58 kDa subunit is capable of folding autonomously into a discrete structure recognizable within the holotoxin and containing the cell binding domain.Journal ArticleResearch Support, Non-U.S. Gov'tSCOPUS: ar.jinfo:eu-repo/semantics/publishe

How We Teach Performance Art : University Courses and Workshop Syllabus

"42 different approaches to transmit the generative source of creativity in live action by internationally experienced practitioners, teachers and theorists of performance art from 21 countries." -- Publisher's website