Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation Export

@article{citeulike:4768993, abstract = {10.1073/pnas.0812771106 Proteins are likely to organize into complexes that assemble and disassemble depending on cellular needs. When \^{a}‰ˆ800 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.}, author = {Narayanaswamy, Rammohan and Levy, Matthew and Tsechansky, Mark and Stovall, Gwendolyn M. and O'Connell, Jeremy D. and Mirrielees, Jennifer and Ellington, Andrew D. and Marcotte, Edward M.}, citeulike-article-id = {4768993}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0812771106}, citeulike-linkout-1 = {http://www.pnas.org/content/0812771106v1//.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/0812771106v1//.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19502427}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19502427}, day = {23}, doi = {10.1073/pnas.0812771106}, journal = {Proceedings of the National Academy of Sciences}, keywords = {quiescence, yeast}, month = {June}, number = {25}, pages = {10147--10152}, posted-at = {2009-11-05 19:32:33}, priority = {2}, title = {Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation}, url = {http://dx.doi.org/10.1073/pnas.0812771106}, volume = {106}, year = {2009} }

TY - JOUR ID - citeulike:4768993 L3 - citeulike-article-id:4768993 N2 - 10.1073/pnas.0812771106 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. IS - 25 JF - Proceedings of the National Academy of Sciences EP - 10152 TI - Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation VL - 106 SP - 10147 KW - quiescence KW - yeast AU - Narayanaswamy, Rammohan AU - Levy, Matthew AU - Tsechansky, Mark AU - Stovall, Gwendolyn AU - O'Connell, Jeremy AU - Mirrielees, Jennifer AU - Ellington, Andrew AU - Marcotte, Edward PY - 2009/06/23/ UR - http://dx.doi.org/10.1073/pnas.0812771106 ER -