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

Previous studies showed that deletion of the CTL leads to aberrant FtsZ assembly that compromises Z-ring formation and cell division (Buske and Levin, 2013) . Replacing the wildtype (WT) CTL with a scrambled sequence variant of the linker preserves Z-ring formation and cell division. In contrast, replacing the CTL with a rigid alpha-helical domain from human betacatenin yielded diffuse FtsZ puncta that compromise Z-ring formation and cell division (Buske and Levin, 2013) . This work underscored the importance of the disordered CTL in FtsZ assembly and Z-ring formation. It also raised several questions regarding the contribution of the intrinsically disordered CTL to the assortment of functions coordinated by FtsZ. Here, we pursue answers to some of these questions by leveraging insights that have emerged through systematic studies of sequence-encoded conformational preferences of intrinsically disordered proteins / regions (Das et al., 2015) .