Evolved sequence features within the intrinsically disordered tail influence FtsZ assembly and bacterial cell division

Megan C. Cohan; Ammon E. Posey; Steven J. Grigsby; Anuradha Mittal; Alex S. Holehouse; Paul J. Buske; Petra A. Levin; Rohit V. Pappu

The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/301622 doi: bioRxiv preprint S3 black and grey curves. These data demonstrate that naturally occurring FtsZ CTT sequences are biased to more positive κ values than expected by random chance. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/301622 doi: bioRxiv preprint S4 dihedral angles. Landscapes can be narrow and smooth (low s and D), narrow and rugged (low s and large D), wide and smooth (high s and low D), or wide and rugged (high s and D). Figure S4 : FtsZ forms protofilaments and polymerization is sensitive to the presence of GTP. (A) FtsZ is a GTPase whose active site is formed by the interface between two FtsZ monomers. The cartoon representation, generated using the VMD software package, is based on the coordinates for FtsZ dimers obtained from the protein data bank (PDB id: 2vxy). In each subunit, residues that make up the GTP binding site are colored in red whereas residues that make up the T7 activation loop are colored in yellow. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/301622 doi: bioRxiv preprint S5 in solution. The larger the aggregates, the greater the intensity of scattered light and aggregates can be a combination of protofilaments and bundled polymers. All rights reserved. No reuse allowed without permission.