RT Journal Article SR Electronic T1 Ubiquitination regulates cytoophidium assembly in Schizosaccharomyces pombe JF bioRxiv FD Cold Spring Harbor Laboratory SP 2021.12.06.470909 DO 10.1101/2021.12.06.470909 A1 Christos Andreadis A1 Tianhao Li A1 Ji-Long Liu YR 2021 UL http://biorxiv.org/content/early/2021/12/07/2021.12.06.470909.abstract AB CTP synthase (CTPS), a metabolic enzyme responsible for the de novo synthesis of CTP, can form filamentous structures termed cytoophidia, which are evolutionarily conserved from bacteria to humans. Here we used Schizosaccharomyces pombe to study the cytoophidium assembly regulation by ubiquitination. We tested the CTP synthase’s capacity to be epigenetically modified by ubiquitin or be affected by the ubiquitination state of the cell, showed that CTPS is immunoprecipitated with ubiquitin, and that ubiquitination is important for the maintenance of the CTPS filamentous structure in fission yeast. We have identified proteins which are in complex with CTPS, including specific ubiquitination regulators which significantly affect CTPS filamentation, and mapped probable ubiquitination targets on CTPS. Furthermore, we discovered that a cohort of deubiquitinating enzymes is significant for the regulation of cytoophidium morphology. Our study provides a framework for the analysis of the effects that ubiquitination and deubiquitination have on the formation of CTPS filaments.Competing Interest StatementThe authors have declared no competing interest.