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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Published inPLoS genetics Vol. 14; no. 10; p. e1007737
Main Authors Zhang, Shanshan, Ding, Kang, Shen, Qing-Ji, Zhao, Suwen, Liu, Ji-Long
Format Journal Article
LanguageEnglish
Published United States Public Library of Science 01.10.2018
Public Library of Science (PLoS)
Subjects
Anatomy & physiology
Asparagine
Aspartate-ammonia ligase
Biochemistry
Biology and Life Sciences
Carbon
Cell cycle
CTP synthase
Cytoplasm
Enzymes
Filamentation
Genes
Genomes
Genomics
Glutamine
Homeostasis
Life sciences
Melanoma
Metabolism
Mutation
Physical Sciences
Physiology
Proteins
Research and Analysis Methods
Saccharomyces cerevisiae
Yeast
United Kingdom > UK
Beijing China
China
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Summary: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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The authors have declared that no competing interests exist.
ISSN:1553-7404
1553-7390
1553-7404
DOI:10.1371/journal.pgen.1007737