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Structure paper

TitleCryo-EM structures of CTP synthase filaments reveal mechanism of pH-sensitive assembly during budding yeast starvation.
Journal, issue, pagesElife, Vol. 10, Year 2021
Publish dateNov 4, 2021
AuthorsJesse M Hansen / Avital Horowitz / Eric M Lynch / Daniel P Farrell / Joel Quispe / Frank DiMaio / Justin M Kollman /
PubMed AbstractMany metabolic enzymes self-assemble into micron-scale filaments to organize and regulate metabolism. The appearance of these assemblies often coincides with large metabolic changes as in ...Many metabolic enzymes self-assemble into micron-scale filaments to organize and regulate metabolism. The appearance of these assemblies often coincides with large metabolic changes as in development, cancer, and stress. Yeast undergo cytoplasmic acidification upon starvation, triggering the assembly of many metabolic enzymes into filaments. However, it is unclear how these filaments assemble at the molecular level and what their role is in the yeast starvation response. CTP Synthase (CTPS) assembles into metabolic filaments across many species. Here, we characterize in vitro polymerization and investigate in vivo consequences of CTPS assembly in yeast. Cryo-EM structures reveal a pH-sensitive assembly mechanism and highly ordered filament bundles that stabilize an inactive state of the enzyme, features unique to yeast CTPS. Disruption of filaments in cells with non-assembly or pH-insensitive mutations decreases growth rate, reflecting the importance of regulated CTPS filament assembly in homeotstasis.
External linksElife / PubMed:34734801 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 7.3 Å
Structure data

24497

7rkh

EMDB-24497, PDB-7rkh:
Yeast CTP Synthase (URA8) tetramer bound to ATP/UTP at neutral pH
Method: EM (single particle) / Resolution: 2.8 Å

24512

7rl0

EMDB-24512, PDB-7rl0:
Yeast CTP Synthase (URA8) Filament bound to ATP/UTP at low pH
Method: EM (single particle) / Resolution: 2.8 Å

24516

7rl5

EMDB-24516, PDB-7rl5:
Yeast CTP Synthase (URA8) filament bound to CTP at low pH
Method: EM (single particle) / Resolution: 3.8 Å

24560

7rmc

EMDB-24560, PDB-7rmc:
Yeast CTP Synthase (Ura7) filament bound to CTP at low pH
Method: EM (single particle) / Resolution: 3.5 Å

24566

7rmf

EMDB-24566, PDB-7rmf:
Substrate-bound Ura7 filament at low pH
Method: EM (single particle) / Resolution: 7.3 Å

24575

7rmk

EMDB-24575, PDB-7rmk:
Yeast CTP Synthase (Ura7) Bundle bound to substrates at low pH
Method: EM (single particle) / Resolution: 6.6 Å

24576

7rmo

EMDB-24576, PDB-7rmo:
Yeast CTP Synthase (Ura7) Bundle bound to Products at low pH
Method: EM (single particle) / Resolution: 7.0 Å

24578

7rmv

EMDB-24578, PDB-7rmv:
Yeast CTP Synthase (Ura7) H360R Filament bound to Substrates
Method: EM (single particle) / Resolution: 6.7 Å

24579

7rnl

EMDB-24579, PDB-7rnl:
Yeast CTP Synthase (Ura7) H360R Filament bound to Substrates
Method: EM (single particle) / Resolution: 3.7 Å

24581

7rnr

EMDB-24581, PDB-7rnr:
Yeast CTP Synthase (Ura8) Bundle Bound to Substrates at Low pH
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-UTP:
URIDINE 5'-TRIPHOSPHATE / UTP*YM / Uridine triphosphate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-CTP:
CYTIDINE-5'-TRIPHOSPHATE / Cytidine triphosphate

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsPROTEIN FIBRIL / glutaminase / amido-ligase / nucleotide metabolism / amino-ligase / glutaminase and amino-ligase / glutaminase and amido-ligase

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