Amnesty for War Crimes in Angola; Principled for a Day?

In April 2012, Angola celebrated ten years of a peace deal which contained an amnesty law. The Angolan government has over the past ten years demonstrated to be unwilling to prosecute perpetrators of war crimes. Potential war criminals currently (still) take important positions in the Angolan government or live as well known public figures in-and outside Angola. The author analyses that especially a lack of domestic interest in doing justice and third countries' interests in Angola's oil reserves might serve as an explanation why up to this moment no justice has been done. The Angolan case illustrates how international actors may react by taking a 'one-day principled position' when it comes to calling for prosecution. Potentially hampering fragile peace negotiations, critique on the blanket nature of the amnesty is before and immediately after the peace process voiced, not to be repeated anytime, anyplace, anywhere. © 2012 Koninklijke Brill NV, Leiden

Institutions, Partnerships and Institutional Change

One of the goals of the Partnership Resource Centre (PRC) is to execute evidence-based research and further develop a theoretical framework on the linkages between partnerships and value chain development (ECSAD 2009). Within the PRC Trajectory on Global Value Chains, this goal was specifi ed into the explicit objective to improve public knowledge of how partnerships shape or organise the process of inclusion of smallholders and small and medium enterprises (SMEs) in (global) value chains, resulting in more local sustainable competitiveness. The global value chains trajectory takes as point of departure the multi tude of institutional constraints that prevent primary producers and SMEs from exploiting local and foreign market opportunities. Apart from adverse climate conditions, limitations in infrastructure, and health and education issues, market-oriented activities are hampered by the lack of an appropriate institutional business environment. Especially the rural poor often have no proper access to, for instance, credit, technology, or land titles, while their market prospects are insecure (Markelova et al 2009; Poulton et al 2006). Value chain partnerships are increasingly considered to be useful vehicles to tackle these limitations, evidenced in the active promotion of particularly bi-partite partnerships between companies and non-governmental organizations (NGOs). The synergy derived from partnership cooperation can overcome failures resulting from unilateral action by actors confined within one of the societal sectors (Kolk et al 2008). By addressing the institutional business environment, partnerships can play a pivotal role in enhancing the chances for primary producers and SMEs to turn themselves into viable suppliers of local or global value chains (Bitzer et al 2011) in support of sustainable, local economic development

Dynamic control of selectivity in the ubiquitination pathway revealed by an ASP to GLU substitution in an intra-molecular salt-bridge network

Ubiquitination relies on a subtle balance between selectivity and promiscuity achieved through specific interactions between ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s). Here, we report how a single aspartic to glutamic acid substitution acts as a dynamic switch to tip the selectivity balance of human E2s for interaction toward E3 RING-finger domains. By combining molecular dynamic simulations, experimental yeast-two-hybrid screen of E2-E3 (RING) interactions and mutagenesis, we reveal how the dynamics of an internal salt-bridge network at the rim of the E2-E3 interaction surface controls the balance between an “open”, binding competent, and a “closed”, binding incompetent state. The molecular dynamic simulations shed light on the fine mechanism of this molecular switch and allowed us to identify its components, namely an aspartate/glutamate pair, a lysine acting as the central switch and a remote aspartate. Perturbations of single residues in this network, both inside and outside the interaction surface, are sufficient to switch the global E2 interaction selectivity as demonstrated experimentally. Taken together, our results indicate a new mechanism to control E2-E3 interaction selectivity at an atomic level, highlighting how minimal changes in amino acid side-chain affecting the dynamics of intramolecular salt-bridges can be crucial for protein-protein interactions. These findings indicate that the widely accepted sequence-structure-function paradigm should be extended to sequence-structure-dynamics-function relationship and open new possibilities for control and fine-tuning of protein interaction selectivity