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Correction: Small Angle X-Ray Scattering Studies of Mitochondrial Glutaminase C Reveal Extended Flexible Regions, and Link Oligomeric State with Enzyme Activity

Year: 2013
Type: erratum
Abstract: Glutaminase C is a key metabolic enzyme, which is unregulated in many cancer systems and believed to play a central role in the Warburg effect, whereby cancer cells undergo changes to an altered metabolic profile.A long-standing hypothesis links enzymatic activity to the protein oligomeric state, hence the study of the solution behavior in general and the oligomer state in particular of glutaminase C is important for the understanding of the mechanism of protein activation and inhibition.In this report, this is extensively investigated in correlation to enzyme concentration or phosphate level, using a high-throughput microfluidic-mixing chip for the SAXS data collection, and we confirm that the oligomeric state correlates with activity.The in-depth solution behavior analysis further reveals the structural behavior of flexible regions of the protein in the dimeric, tetrameric and octameric state and investigates the C-terminal influence on the enzyme solution behavior.Our data enable SAXS-based rigid body modeling of the full-length tetramer states, thereby presenting the first ever experimentally derived structural model of mitochondrial glutaminase C including the N-and C-termini of the enzyme.
Source: PLoS ONE
DOI: 10.1371/annotation/80d64df5-065e-4be9-a4e8-31c4cba67114
Authors: Magda Møller, Søren S. Nielsen, Sekar Ramachandran, Li Yunxing, Giancarlo Tria, Werner Streicher, Maxim V. Petoukhov, Richard A. Cerione, Richard E. Gillilan, Bente Vestergaard
Institutions: University of Copenhagen, Cornell University, Cornell High Energy Synchrotron Source, Universität Hamburg, Deutsches Elektronen-Synchrotron DESY, European Molecular Biology Laboratory, European Molecular Biology Laboratory, Novo Nordisk Foundation, University of Oulu
Language: English
Open Access status: gold
Estimated APC paid: $2,382
Funders: National Science Foundation, Danmarks Tekniske Universitet, Faculty of Health and Medical Sciences, University of Western Australia, National Institutes of Health, Det Sundhedsvidenskabelige Fakultet, Københavns Universitet, National Institute of General Medical Sciences, Division of Materials Research, National Center for Research Resources
Awards: G1488452202, G1641640346, G367921431, G3976199993, Operation of the Cornell High Energy Synchrotron Source (CHESS), G5825187129, G9000231267
OpenAlex ID: W4242218221
Cites: 27
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Related to: 10