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The copyright holder for this preprint (which was not peer-reviewed) is the author/funder.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 lowered sequence complexity. Sequence complexity is also lowered by using a simplified amino acid composition as we have done with the CTT sequences that are based on a reduced amino acid library. In eukaryotic systems, ubiquitinated substrates engage productively with the proteasome if and only if they have low sequence complexity tags at their termini (Kraut et al., 2012; Schrader et al., 2011) . Accordingly, we quantified the sequence complexities of each of the designed CTTs based on the WT and reduced amino acid alphabets. Here, we use the Lempel-Ziv (LZ) measure of complexity (Lempel and Ziv, 1976 ) that has been used in previous analysis of IDPs / IDRs Romero et al., 2000) . Interestingly, we find that the variants that have low cellular levels in B. subtilis (Figure 3B & 6B) also have the lowest LZ sequence complexity in their CTT sequences ( Figure 6E) . The sequence complexity of CTT sequences is lowered either by increasing or decreasing κ within the CTT, for the WT amino acid composition or by using a reduced alphabet for the amino acid composition.