期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 106, 期 25, 页码 10147-10152出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0812771106
关键词
aggregation; metabolism; microscopy; proteomics; quiescence
资金
- National Science Foundation [IIS-0325116, EIA-0219061]
- National Institutes of Health [GM06779-01, GM076536-01]
- Welch Foundation [F1515]
- Packard Fellowship
Proteins are likely to organize into complexes that assemble and disassemble depending on cellular needs. When approximate to 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.
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