De historica van de juristen en de rechtenfaculteiten : rechtshistorici uit de Lage Landen (15) : interview met Hilde Symoens

This article is an interview with Hilde Symoens, the fifteenth in a series of Pro Memorie talks with retired Dutch and Belgian legal historians. Born in Brussels in 1943, Hilde Symoens spent part of her youth in Congo, where her parents, still in the colonial era, worked as teachers, She returned with her mother to Belgium in 1958 and started her university studies at Ghent University in 1960. As her father kept on being responsible for the Belgian schools in decolonized Congo, the colonial experience and the more general idea that the world was more than just the village one lives in, were important for her personal view of the world. At Ghent University, Hilde Symoens studied history and engaged in a PhD project on the Low Countries students at the late medieval and early modern university of Orléans. It was the start for o whole scientific career on the prosopography and the social roles of jurists. As a historian, not a jurist herself, she studied particularly ‘external legal history’. She married Ghent professor of medicine Leo De Ridder, was full professor at the Vrije Universiteit Amsterdam and at Ghent University. She was one of the first women making career as history professor and talks on the incomprehension she met on her way

Specific Sequences in the N-terminal Domain of Human Small Heat Shock Protein HSPB6 Dictate Preferential Heterooligomerization with the Orthologue HSPB1

Small heat-shock proteins (sHSPs) are a conserved group of molecular chaperones with important roles in cellular proteostasis. Although sHSPs are characterized by their small monomeric weight, they typically assemble into large polydisperse oligomers that vary in both size and shape but are principally composed of dimeric building blocks. These assemblies can include different sHSP orthologues, creating additional complexity that may affect chaperone activity. However, the structural and functional properties of such hetero-oligomers are poorly understood. We became interested in hetero-oligomer formation between human heat-shock protein family B (small) member 1 (HSPB1) and HSPB6, which are both highly expressed in skeletal muscle. When mixed in vitro, these two sHSPs form a polydisperse oligomer array composed solely of heterodimers, suggesting preferential association that is determined at the monomer level. Previously, we have shown that the sHSP N-terminal domains (NTDs), which have a high degree of intrinsic disorder, are essential for the biased formation. Here we employed iterative deletion mapping to elucidate how the NTD of HSPB6 influences its preferential association with HSPB1 and show that this region has multiple roles in this process. First, the highly conserved motif RLFDQXFG is necessary for subunit exchange among oligomers. Second, a site ∼20 residues downstream of this motif determines the size of the resultant hetero-oligomers. Third, a region unique to HSPB6 dictates the preferential formation of heterodimers. In conclusion, the disordered NTD of HSPB6 helps regulate the size and stability of hetero-oligomeric complexes, indicating that terminal sHSP regions define the assembly properties of these proteins

De verdedigingswerken van de Romeinse legerplaatsen op de Hunerberg, Nijmegen-Oost : archeologisch onderzoek

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