Microbial relatives of seed storage proteins: conservation of motifs in a functionally diverse superfamily of enzymes

Plant storage proteins comprise a major part of the human diet. Sequence analysis has revealed that these proteins probably share a common ancestor with a fungal oxalate decarboxylase and/or related bacterial genes. Additionally, all these proteins share a central core sequence with several other functionally diverse enzymes and binding proteins, many of which are associated with synthesis of the extracellular matrix during sporulation/encystment. A possible prokaryotic relative of this sequence is a bacterial protein (SASP) known to bind to DNA and thereby protect spores from extreme environmental conditions. This ability to maintain cell viability during periods of dehydration in spores and seeds may relate to absolute conservation of residues involved in structure determination.

Oi! Oi! Oi! : class locality and British punk

This article looks at the controversial music genre Oi! in relation to youth cultural identity in late 1970s’ and early 1980s’ Britain. As a form of British punk associated with skinheads, Oi! has oft-been dismissed as racist and bound up in the politics of the far right. It is argued here, however, that such a reading is too simplistic and ignores the more complex politics contained both within Oi! and the various youth cultural currents that revolved around the term ‘punk’ at this time. Taking as its starting point the Centre for Contemporary Cultural Studies’ conception of youth culture as a site of potential ‘resistance’, the article explores the substance and motifs of Oi!’s protest to locate its actual and perceived meaning within a far wider political and socio-economic context. More broadly, it seeks to demonstrate the value of historians examining youth culture as a formative and contested socio-cultural space within which young people discover, comprehend, and express their desires, opinions, and disaffections.

Self-assembly of a dual functional bioactive peptide amphiphile incorporating both matrix metalloprotease substrate and cell adhesion motifs

We describe a bioactive lipopeptide that combines the capacity to promote the adhesion and subsequent self-detachment of live cells, using template-cell-environment feedback interactions. This self-assembling peptide amphiphile comprises a diene-containing hexadecyl lipid chain (C16e) linked to a matrix metalloprotease-cleavable sequence, Thr-Pro-Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln, and contiguous with a cell-attachment and signalling motif, Arg-Gly-Asp-Ser. Biophysical characterisation revealed that the PA self-assembles into 3 nm diameter spherical micelles above a critical aggregation concentration (cac). In addition, when used in solution at 5–150 nM (well below the cac), the PA is capable of forming film coatings that provide a stable surface for human corneal fibroblasts to attach and grow. Furthermore, these coatings were demonstrated to be sensitive to metalloproteases expressed endogenously by the attached cells, and consequently to elicit the controlled detachment of cells without compromising their viability. As such, this material constitutes a novel class of multi-functional coating for both fundamental and clinical applications in tissue engineering.