Project: The type VI secretion system of Francisella tularensis
PI: Anders Sjöstedt
The aim is to delineate the regulation of assembly and the functions of the components of the Type VI secretion systems (T6SS) of Francisella tularensis (Ft). Ft encodes an atypical T6SS, which allows this highly virulent, intracellular bacterium to invade and replicate within the cytosol of eukaryotic cells and the T6SS is thereby essential for Ft virulence. While T6SSs have been the focus of an intense research effort for over a decade, our understanding is still incomplete regarding many of the functions of T6SSs in general and that of Ft in particular.
The research will be carried out by generating specific mutants and constructs encoding tagged T6SS components. These will then be tested by a variety of techniques, including several microscopic techniques, to detect the localization and secretion of the proteins, as well as their protein interaction partners. One focus will be on the baseplate, the foundation on which the external part of the machinery rests. Detailed structural knowledge is very limited regarding the Ft baseplate, a consequence of the low sequence identity between Ft T6SS components and those of prototypic T6SSs. We are currently conducting detailed analysis by means of for example two-hybrid interaction analysis, immunoprecipitation, ascorbate peroxidase 2 (APEX)-tagging, and confocal and electron microscopy methods.
Application deadline: 7 January 2021. Continue to read for all details and how to apply.
We have recently identified a critical role of the ClpB chaperone (Alam et al., Scientific Reports, 2018) and made the novel finding that its role for the control of T6S is dissociated from its role as essential for the heat shock response (Alam et al., Plos Pathogens, 2020). To further understand the underlying mechanisms is one aim. Much Ft research has focused on the control of T6SS assembly in the environmental bacterium F. novicida. Therefore, another aim will be to study clinically important Ft subspecies to see if the mechanism is conserved, with a special focus on ClpB and its role for the assembly/disassembly of the T6SS.
- https://www.umu.se/en/work-with-us/open-positions/postdoctoral-position_367476/ (in English)
- https://www.umu.se/jobba-hos-oss/lediga-jobb/postdoktor_367476/ (in Swedish)
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