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Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ
FtsZ is the bacterial tubulin homolog that forms Z-ring, which is a dynamic ring like structure, at the site of cell division to assemble the divisome and generate constrictive force for septum formation. SepF is the key protein that anchors the constricting Z-ring to the protruding septal membrane in Mycobacterium tuberculosis, via its interaction with the intrinsically disordered C-terminal tail of FtsZ. We characterized the cytosolic component of mycobacterial SepF, and its interaction with cognate FtsZ, using negative stained electron microscopy, small angle X-ray scattering, 90 degree angle light scattering and isothermal titration calorimetry. Cytoplasmic domain of SepF from M. tuberculosis, like its other homologs, form large ring-shaped polymer. interaction between the C-terminal part of FtsZ and cytoplasmic SepF was confirmed by isothermal titration calorimetry. SepF induces bundling of FtsZ in the presence of nucleotides. Our results are discussed in light of the present understanding of divisome assembling
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