Filamentation of asparagine synthetase in Saccharomyces cerevisiae

Asparagine synthetase (ASNS) and CTP synthase (CTPS) are two metabolic enzymes crucial for glutamine homeostasis. A genome-wide screening in Saccharomyces cerevisiae reveal that both ASNS and CTPS form filamentous structures termed cytoophidia. Although CTPS cytoophidia were well documented in recen...

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Main Authors: Zhang, S, Ding, K, Shen, Q, Zhao, S, Liu, J
Format: Journal article
Language:English
Published: Public Library of Science 2018
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author Zhang, S
Ding, K
Shen, Q
Zhao, S
Liu, J
author_facet Zhang, S
Ding, K
Shen, Q
Zhao, S
Liu, J
author_sort Zhang, S
collection OXFORD
description Asparagine synthetase (ASNS) and CTP synthase (CTPS) are two metabolic enzymes crucial for glutamine homeostasis. A genome-wide screening in Saccharomyces cerevisiae reveal that both ASNS and CTPS form filamentous structures termed cytoophidia. Although CTPS cytoophidia were well documented in recent years, the filamentation of ASNS is less studied. Using the budding yeast as a model system, here we confirm that two ASNS proteins, Asn1 and Asn2, are capable of forming cytoophidia in diauxic and stationary phases. We find that glucose deprivation induces ASNS filament formation. Although ASNS and CTPS form distinct cytoophidia with different lengths, both structures locate adjacently to each other in most cells. Moreover, we demonstrate that the Asn1 cytoophidia colocalize with the Asn2 cytoophidia, while Asn2 filament assembly is largely dependent on Asn1. In addition, we are able to alter Asn1 filamentation by mutagenizing key sites on the dimer interface. Finally, we show that ASN1D330V promotes filamentation. The ASN1D330V mutation impedes cell growth in an ASN2 knockout background, while growing normally in an ASN2 wild-type background. Together, this study reveals a connection between ASNS and CTPS cytoophidia and the differential filament-forming capability between two ASNS paralogs.
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spelling oxford-uuid:c166b49b-f134-434e-a2c1-21c4ab2c72f12022-03-27T06:01:10ZFilamentation of asparagine synthetase in Saccharomyces cerevisiaeJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c166b49b-f134-434e-a2c1-21c4ab2c72f1EnglishSymplectic Elements at OxfordPublic Library of Science2018Zhang, SDing, KShen, QZhao, SLiu, JAsparagine synthetase (ASNS) and CTP synthase (CTPS) are two metabolic enzymes crucial for glutamine homeostasis. A genome-wide screening in Saccharomyces cerevisiae reveal that both ASNS and CTPS form filamentous structures termed cytoophidia. Although CTPS cytoophidia were well documented in recent years, the filamentation of ASNS is less studied. Using the budding yeast as a model system, here we confirm that two ASNS proteins, Asn1 and Asn2, are capable of forming cytoophidia in diauxic and stationary phases. We find that glucose deprivation induces ASNS filament formation. Although ASNS and CTPS form distinct cytoophidia with different lengths, both structures locate adjacently to each other in most cells. Moreover, we demonstrate that the Asn1 cytoophidia colocalize with the Asn2 cytoophidia, while Asn2 filament assembly is largely dependent on Asn1. In addition, we are able to alter Asn1 filamentation by mutagenizing key sites on the dimer interface. Finally, we show that ASN1D330V promotes filamentation. The ASN1D330V mutation impedes cell growth in an ASN2 knockout background, while growing normally in an ASN2 wild-type background. Together, this study reveals a connection between ASNS and CTPS cytoophidia and the differential filament-forming capability between two ASNS paralogs.
spellingShingle Zhang, S
Ding, K
Shen, Q
Zhao, S
Liu, J
Filamentation of asparagine synthetase in Saccharomyces cerevisiae
title Filamentation of asparagine synthetase in Saccharomyces cerevisiae
title_full Filamentation of asparagine synthetase in Saccharomyces cerevisiae
title_fullStr Filamentation of asparagine synthetase in Saccharomyces cerevisiae
title_full_unstemmed Filamentation of asparagine synthetase in Saccharomyces cerevisiae
title_short Filamentation of asparagine synthetase in Saccharomyces cerevisiae
title_sort filamentation of asparagine synthetase in saccharomyces cerevisiae
work_keys_str_mv AT zhangs filamentationofasparaginesynthetaseinsaccharomycescerevisiae
AT dingk filamentationofasparaginesynthetaseinsaccharomycescerevisiae
AT shenq filamentationofasparaginesynthetaseinsaccharomycescerevisiae
AT zhaos filamentationofasparaginesynthetaseinsaccharomycescerevisiae
AT liuj filamentationofasparaginesynthetaseinsaccharomycescerevisiae