E-Poster Presentation Australian Society for Microbiology Annual Scientific Meeting 2021

Multiple CetZ tubulin-like proteins influence swimming motility in the archaeon Haloferax volcanii (#305)

Hannah J Brown 1 , Solenne Ithurbide 1 , Iain G Duggin 1
  1. University of Technology Sydney, Randwick, NSW, Australia

CetZs are an Archaea-specific family of tubulin superfamily proteins (Duggin et al., 2015). Haloferax volcanii has six CetZs as well as two related FtsZ proteins needed for cell division. Typical of cytoskeletal proteins, the CetZs have been implicated in multiple cellular functions. These include motility, control of cell shape, and possibly cell division. The most highly conserved of the CetZ proteins, CetZ1, is necessary for H. volcanii discoid-shaped cells to develop into rods, increasing the rate of swimming motility. However, individual deletion of CetZ2-6 does not have any substantial effect on motility under standard laboratory conditions, and the biological functions of these proteins still remain unknown. CetZ2 is the second most highly conserved of the CetZs among archaeal species, but published RNAseq data and our western blots show it is expressed at a very low level in standard conditions. However, we found that overexpression of CetZ2 causes H. volcanii to become hypermotile, and that CetZ2 overexpression induced hypermotility is dependent on CetZ1. It is possible that CetZ1 is important for a basal level of motility, which CetZ2 is not required for, and that CetZ2 may be upregulated in certain conditions in order to enhance motility via an inducible motility pathway. Future studies will determine how CetZ1 and CetZ2 are involved in archaeal motility, by understanding their relationship with motility components like the archaellum and chemotaxis proteins.