Please use this identifier to cite or link to this item: https://doi.org/10.1002/cm.20526
Title: Bacillus anthracis tubulin-related protein Ba-TubZ assembles force-generating polymers
Authors: Srinivasan, R. 
Mishra, M.
Leong, F.Y.
Chiam, K.-H.
Balasubramanian, M.
Keywords: Bacteria
Cytoskeleton
Fission yeast
Plasmid segregation
Virulence
Issue Date: Sep-2011
Source: Srinivasan, R., Mishra, M., Leong, F.Y., Chiam, K.-H., Balasubramanian, M. (2011-09). Bacillus anthracis tubulin-related protein Ba-TubZ assembles force-generating polymers. Cytoskeleton 68 (9) : 501-511. ScholarBank@NUS Repository. https://doi.org/10.1002/cm.20526
Abstract: Pathogenicity of Bacillus anthracis depends on the faithful inheritance of plasmid pXO1, in a process that requires the plasmid encoded tubulin-related protein Ba-TubZ. Here we show, using heterologous expression in Schizosaccharomyces pombe, that Ba-TubZ assembles into a dynamic polymer in the absence of other B. anthracis proteins and can generate force capable of deforming the fission yeast nuclear envelope. The polymer bundles contain 27 ± 15 protofilaments/μm assuming that each protofilament spans the entire length. Thinner appearing buckled and thicker appearing straight filaments of Ba-TubZ were both capable of inducing nuclear envelope deformation. Unlike the related protein Bt-TubZ from Bacillus thuringiensis, which undergoes treadmilling upon expression in fission yeast, Ba-TubZ polymers did not undergo detectable treadmilling. Instead, in fluorescence recovery after photobleaching experiments, it displayed a different turnover behavior characterized by moderate fluorescence recovery along the entire length of the polymer. Modeling Ba-TubZ bundles as Euler-Bernoulli beams that buckle under compressive loads when pushed against the nuclear envelope allowed us to estimate that Ba-TubZ generates forces in the order of 1-10 nN. We propose that polymerization based filament elongation and force generation might aid faithful segregation of the virulence plasmid. © 2011 Wiley-Liss, Inc.
Source Title: Cytoskeleton
URI: http://scholarbank.nus.edu.sg/handle/10635/116932
ISSN: 19493584
DOI: 10.1002/cm.20526
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