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2016 Fall course offering list 08/12/2016
2016 MBAS Admission Announcement (early-decision deadline: 1/31, final deadline: 3/31) 01/20/2016
2016 Spring course offering list 12/10/2015
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Devanand D. Bondage, Jer-Sheng Lin, Lay-Sun Ma, Chih-Horng Kuo and Erh-Min Lai* (2016) VgrG C terminus confers the type VI effector transport specificity and is required for binding with PAAR and adaptor–effector complex- Proceedings of the National Academy of Sciences of the United States of America: doi:10.1073/pnas.1600428113.

Type VI secretion system (T6SS) is a molecular weapon used by many Gram-negative bacteria to inject effectors into eukaryotic host cells or competing prokaryotes for bacterial survival and fitness. T6SS involves multiple strategies for effector delivery via fusion or interaction of effectors to structural components of the phage tail-like structure. However, the identity of the molecular components and mechanisms that governs the delivery of type VI effectors remains limited. The research team (Bondage et al.) at the Institute of Plant and Microbial Biology studied the delivery mechanism of antibacterial type VI effectors, namely Tde1 and Tde2 DNase toxins, in Agrobacterium tumefaciens. They identified the protein components named as spike (VgrG1 and VgrG2 protein), adaptor/chaperone (Tap-1 and Atu3641), and a sharp tip (PAAR) are required for delivery of cognate Tde toxin. Importantly, the divergent C-terminus of VgrG1 and VgrG2 spike proteins governs the Tde toxin delivery specificity. In-depth genetic and biochemical evidence demonstrated that VgrG1 C-terminus is the molecular determinant required for interacting with a specific adaptor/chaperone protein and PAAR tip protein to govern Tde1 translocation across bacterial membranes and delivery into target cells for antibacterial activity. Further genome-wide survey discovered the widespread presence of these genetic modules in various Proteobacteria, suggesting a conserved mechanism in type VI effector delivery.




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