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ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae

Asparagine synthetase (ASNS) and CTP synthase (CTPS) are two metabolic enzymes that catalyze the biosynthesis of asparagine and CTP, respectively. Both CTPS and ASNS have been identified to form cytoophidia in Saccharomyces cerevisiae. Glutamine is a common substrate for both these enzymes, and they...

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Detalles Bibliográficos
Autores principales: Zhang, Shanshan, Feng, Han-Chao, Liu, Ji-Long
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8022725/
https://www.ncbi.nlm.nih.gov/pubmed/33561249
http://dx.doi.org/10.1093/g3journal/jkaa060
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author Zhang, Shanshan
Feng, Han-Chao
Liu, Ji-Long
author_facet Zhang, Shanshan
Feng, Han-Chao
Liu, Ji-Long
author_sort Zhang, Shanshan
collection PubMed
description Asparagine synthetase (ASNS) and CTP synthase (CTPS) are two metabolic enzymes that catalyze the biosynthesis of asparagine and CTP, respectively. Both CTPS and ASNS have been identified to form cytoophidia in Saccharomyces cerevisiae. Glutamine is a common substrate for both these enzymes, and they play an important role in glutamine homeostasis. Here, we find that the ASNS cytoophidia are shorter than the CTPS cytoophidia, and that disruption of ASNS shortens the length of CTPS cytoophidia. However, the deletion of CTPS has no effect on the formation and length of ASNS cytoophidia, or on the ASNS protein level. We also find that Asn1 overexpression induces the formation of a multi-dot structure in diauxic phase which suggests that the increased protein level may trigger cytoophidia formation. Collectively, our results reveal a connection between ASNS cytoophidia and CTPS cytoophidia.
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spelling pubmed-80227252021-04-09 ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae Zhang, Shanshan Feng, Han-Chao Liu, Ji-Long G3 (Bethesda) Investigation Asparagine synthetase (ASNS) and CTP synthase (CTPS) are two metabolic enzymes that catalyze the biosynthesis of asparagine and CTP, respectively. Both CTPS and ASNS have been identified to form cytoophidia in Saccharomyces cerevisiae. Glutamine is a common substrate for both these enzymes, and they play an important role in glutamine homeostasis. Here, we find that the ASNS cytoophidia are shorter than the CTPS cytoophidia, and that disruption of ASNS shortens the length of CTPS cytoophidia. However, the deletion of CTPS has no effect on the formation and length of ASNS cytoophidia, or on the ASNS protein level. We also find that Asn1 overexpression induces the formation of a multi-dot structure in diauxic phase which suggests that the increased protein level may trigger cytoophidia formation. Collectively, our results reveal a connection between ASNS cytoophidia and CTPS cytoophidia. Oxford University Press 2021-01-11 /pmc/articles/PMC8022725/ /pubmed/33561249 http://dx.doi.org/10.1093/g3journal/jkaa060 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of Genetics Society of America. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Investigation
Zhang, Shanshan
Feng, Han-Chao
Liu, Ji-Long
ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae
title ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae
title_full ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae
title_fullStr ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae
title_full_unstemmed ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae
title_short ASNS disruption shortens CTPS cytoophidia in Saccharomyces cerevisiae
title_sort asns disruption shortens ctps cytoophidia in saccharomyces cerevisiae
topic Investigation
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8022725/
https://www.ncbi.nlm.nih.gov/pubmed/33561249
http://dx.doi.org/10.1093/g3journal/jkaa060
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