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Bacteria deploy rearrangement hotspot (Rhs) proteins as toxic effectors against both prokaryotic and eukaryotic target cells. Rhs proteins are characterized by YD-peptide repeats, which fold into a large β-cage structure that encapsulates the C-terminal toxin domain. Here, we show that Rhs effectors are essential for type VI secretion system (T6SS) activity in Enterobacter cloacae (ECL). ECL rhs− mutants do not kill Escherichia coli target bacteria and are defective for T6SS-dependent export of hemolysin-coregulated protein (Hcp). The RhsA and RhsB effectors of ECL both contain Pro−Ala−Ala−Arg (PAAR) repeat domains, which bind the β-spike of trimeric valine−glycine repeat protein G (VgrG) and are important for T6SS activity in other bacteria. Truncated RhsA that retains the PAAR domain is capable of forming higher-order, thermostable complexes with VgrG, yet these assemblies fail to restore secretion activity to ∆rhsA ∆rhsB mutants. Full T6SS-1 activity requires Rhs that contains N-terminal transmembrane helices, the PAAR domain, and an intact β-cage. Although ∆rhsA ∆rhsB mutants do not kill target bacteria, time-lapse microscopy reveals that they assemble and fire T6SS contractile sheaths at ∼6% of the frequency of rhs+ cells. Therefore, Rhs proteins are not strictly required for T6SS assembly, although they greatly increase secretion efficiency. We propose that PAAR and the β-cage provide distinct structures that promote secretion. PAAR is clearly sufficient to stabilize trimeric VgrG, but efficient assembly of T6SS-1 also depends on an intact β-cage. Together, these domains enforce a quality control checkpoint to ensure that VgrG is loaded with toxic cargo before assembling the secretion apparatus.

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Gram-negative bacteria use type VI secretion systems deliver toxic effector proteins directly into neighboring competitors. Secreting cells also produce specific immunity proteins that neutralize effector activities to prevent autointoxication.

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Disaster risk management (DRM) is undergoing noteworthy changes, reflecting the broader shifts in global and local levels of governance. At the global level two significant changes are of interest: (1) the shift from monolithic structures of global governance to a wide range of organizations that can be brought together for specific purposes and (2) the emergence of a globalized system of DRM, with technological, organizational, and institutional capacities enhancing DRM's ability as a unit in near real time across the globe. At the local level there is an increase in ability to govern and develop creative solutions for complex problems that follow rapid urbanization. The importance of getting the global-local interface to work in tandem has been highlighted by recent hazard events, such as the 2011 Tohoku Earthquake and Tsunami. From a broad view of global and local shifts, a strategic role is becoming clearer at the national level for enhancing the relationships between the global and local levels. Through the influence of a globalized system of DRM, the local level can significantly improve its capacity without the heavy investment that might have been required to develop these capacities in isolation. One key to achieving this is a diffusion of DRM higher education, supported by an enhanced system of information flow.