TY - JOUR
T1 - Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation
AU - Narayanaswamy, Rammohan
AU - Levy, Matthew
AU - Tsechansky, Mark
AU - Stovall, Gwendolyn M.
AU - O'Connell, Jeremy D.
AU - Mirrielees, Jennifer
AU - Ellington, Andrew D.
AU - Marcotte, Edward M.
PY - 2009/6/23
Y1 - 2009/6/23
N2 - 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.
AB - 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.
KW - Aggregation
KW - Metabolism
KW - Microscopy
KW - Proteomics
KW - Quiescence
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U2 - 10.1073/pnas.0812771106
DO - 10.1073/pnas.0812771106
M3 - Article
C2 - 19502427
AN - SCOPUS:67649875630
SN - 0027-8424
VL - 106
SP - 10147
EP - 10152
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 25
ER -