CTP synthase forms cytoophidia in archaea

Zhou, S.; Xiang, H.; Liu, J.-L.

doi:10.1101/830091

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bioRxiv · 10.1101/830091

CTP synthase forms cytoophidia in archaea

Zhou, S.·Xiang, H.·Liu, J.-L.

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Abstract

CTP synthase (CTPS) is an important metabolic enzyme that catalyzes the rate-limiting reaction of de novo synthesis of the nucleotide CTP. Since 2010, a series of studies have demonstrated that CTPS can form filamentous structures termed cytoophidia in bacteria and eukaryotes. However, it remains unknown whether cytoophidia exist in archaea, the third domain of life. Using Haloarcula hispanica as a model system, here we demonstrate that CTPS forms distinct intracellular compartments in archaeal cells. Under stimulated emission depletion (STED) microscopy, we find that some HhCTPS compartments have elongated filamentous structures, resembling cytoophidia in bacteria and eukaryotes. When Haloarcula cells are cultured in low-salt medium, the occurrence of cytoophidia increases dramatically. Moreover, overexpression of CTPS or glutamine analog treatment promotes cytoophidium assembly in H. hispanica. Our study reveals that CTPS forms cytoophidia in all three domains of life, suggesting that this is an ancient property of CTPS.

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Zhou, S., Xiang, H., Liu, J.-L.. 2019-11-04. CTP synthase forms cytoophidia in archaea. https://doi.org/10.1101/830091

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