Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation

Rammohan Narayanaswamy, Matthew Levy, Mark Tsechansky, Gwendolyn M. Stovall, Jeremy D. O'Connell, Jennifer Mirrielees, Andrew D. Ellington, Edward M. Marcotte

Research output: Contribution to journalArticle

206 Scopus citations

Abstract

Proteins are likely to organize into complexes that assemble and disassemble depending on cellular needs. When ≈800 yeast strains expressing GFP-tagged proteins were grown to stationary phase, a surprising number of proteins involved in intermediary metabolism and stress response were observed to form punctate cytoplasmic foci. The formation of these discrete physical structures was confirmed by immunofluorescence and mass spectrometry of untagged proteins. The purine biosynthetic enzyme Ade4-GFP formed foci in the absence of adenine, and cycling between punctate and diffuse phenotypes could be controlled by adenine subtraction and addition. Similarly, glutamine synthetase (Gln1-GFP) foci cycled reversibly in the absence and presence of glucose. The structures were neither targeted for vacuolar or autophagosome degradation nor colocalized with P bodies or major organelles. Thus, upon nutrient depletion we observe widespread protein assemblies displaying nutrient-specific formation and dissolution.

Original languageEnglish (US)
Pages (from-to)10147-10152
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue number25
DOIs
StatePublished - Jun 23 2009

Keywords

  • Aggregation
  • Metabolism
  • Microscopy
  • Proteomics
  • Quiescence

ASJC Scopus subject areas

  • General

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    Narayanaswamy, R., Levy, M., Tsechansky, M., Stovall, G. M., O'Connell, J. D., Mirrielees, J., Ellington, A. D., & Marcotte, E. M. (2009). Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation. Proceedings of the National Academy of Sciences of the United States of America, 106(25), 10147-10152. https://doi.org/10.1073/pnas.0812771106