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

However, recent studies have demonstrated that while IDRs / IDPs may make up a small fraction of proteins / protein regions in bacterial proteomes when compared to eukaryotic ones, the synergies between IDRs and folded domains contribute directly to an assortment of functions. Prominent bacterial IDRs / IDPs include proteins involved in regulating cell division (Buske and Levin, 2013; Buske et al., 2015) , DNA replication (Kozlov et al., 2015; Shereda et al., 2008) , protein and RNA quality control (Ait- Foit et al., 2013; Jakob et al., 2014; Quan et al., 2014; Reichmann et al., 2012; Updegrove et al., 2016) , bacterial warfare (Bonsor et al., 2008; Hecht et al., 2009; Papadakos et al., 2015) , biofilm formation (Gruszka et al., 2016; Gu et al., 2017; Whelan and Potts, 2015) , and chemotaxis (Daughdrill et al., 1997; Dedmon et al., 2002; Ding et al., 2009) . These findings raise a key dimerization step and the elongation of polymers (Caplan and Erickson, 2003; Romberg et al., 2001) . Filaments can associate laterally with one another to form bundles (Gonzalez et al., 2005; Romberg and Levin, 2003) . GTP hydrolysis promotes the bending of laterally associated polymers to form wreath-like structures that vary in thickness around the circumference (den Blaauwen et al., 2017) .