Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster

Autor: Chalongrat Noree, James E. Wilhelm, Brian K. Sato, Risa M. Broyer
Rok vydání: 2010
Předmět:
Cytidine triphosphate
Saccharomyces cerevisiae Proteins
Prions
Protein Conformation
1.1 Normal biological development and functioning
Recombinant Fusion Proteins
Saccharomyces cerevisiae
Eukaryotic Initiation Factor-2
Guanosine
macromolecular substances
Medical and Health Sciences
chemistry.chemical_compound
Underpinning research
Report
Glutamate synthase
Animals
Drosophila Proteins
Carbon-Nitrogen Ligases
Translation factor
Enzyme Inhibitors
Research Articles
Neurons
Protein Synthesis Inhibitors
biology
ATP synthase
fungi
food and beverages
Cell Biology
Biological Sciences
biology.organism_classification
Staurosporine
Nucleotidyltransferases
Eukaryotic Initiation Factor-2B
Drosophila melanogaster
chemistry
Biochemistry
Cytoplasm
biology.protein
Cytoophidium
Generic health relevance
Developmental Biology
Zdroj: The Journal of cell biology, vol 190, iss 4
The Journal of Cell Biology
Popis: A screen for GFP-tagged yeast proteins that can assemble into visible structures reveals four new filamentous structures in the cytoplasm formed by metabolic enzymes and translation factors.
The discovery of large supramolecular complexes such as the purinosome suggests that subcellular organization is central to enzyme regulation. A screen of the yeast GFP strain collection to identify proteins that assemble into visible structures identified four novel filament systems comprised of glutamate synthase, guanosine diphosphate–mannose pyrophosphorylase, cytidine triphosphate (CTP) synthase, or subunits of the eIF2/2B translation factor complex. Recruitment of CTP synthase to filaments and foci can be modulated by mutations and regulatory ligands that alter enzyme activity, arguing that the assembly of these structures is related to control of CTP synthase activity. CTP synthase filaments are evolutionarily conserved and are restricted to axons in neurons. This spatial regulation suggests that these filaments have additional functions separate from the regulation of enzyme activity. The identification of four novel filaments greatly expands the number of known intracellular filament networks and has broad implications for our understanding of how cells organize biochemical activities in the cytoplasm.
Databáze: OpenAIRE