title: Granules harboring translationally active mRNAs provide a platform for P-body formation following stress.
abstract: The localization of mRNA to defined cytoplasmic sites in eukaryotic cells not only allows localized protein production but also determines the fate of mRNAs. For instance, translationally repressed mRNAs localize to P-bodies and stress granules where their decay and storage, respectively, are directed. Here, we find that several mRNAs are localized to granules in unstressed, actively growing cells. These granules play a key role in the stress-dependent formation of P-bodies. Specific glycolytic mRNAs are colocalized in multiple granules per cell, which aggregate during P-body formation. Such aggregation is still observed under conditions or in mutants where P-bodies do not form. In unstressed cells, the mRNA granules appear associated with active translation; this might enable a coregulation of protein expression from the same pathways or complexes. Parallels can be drawn between this coregulation and the advantage of operons in prokaryotic systems.
authors.affiliation: Faculty of Life Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PT, UK.
authors.forename: Jennifer
authors.initials: J
authors.lastname: Lui
authors.affiliation: Faculty of Life Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PT, UK.
authors.forename: Lydia M
authors.initials: LM
authors.lastname: Castelli
authors.affiliation: Faculty of Life Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PT, UK.
authors.forename: Mariavittoria
authors.initials: M
authors.lastname: Pizzinga
authors.affiliation: Faculty of Life Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PT, UK.
authors.forename: Clare E
authors.initials: CE
authors.lastname: Simpson
authors.affiliation: Faculty of Life Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PT, UK.
authors.forename: Nathaniel P
authors.initials: NP
authors.lastname: Hoyle
authors.affiliation: Faculty of Life Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PT, UK.
authors.forename: Kathryn L
authors.initials: KL
authors.lastname: Bailey
authors.affiliation: Biosciences Department, Faculty of Health and Wellbeing, Sheffield Hallam University, Howards Street, Sheffield S1 1WB, UK.
authors.forename: Susan G
authors.initials: SG
authors.lastname: Campbell
authors.affiliation: Faculty of Life Sciences, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PT, UK. Electronic address: mark.p.ashe@manchester.ac.uk.
authors.forename: Mark P
authors.initials: MP
authors.lastname: Ashe
mesh_terms: D000596:Amino Acids / Q000172:deficiency; D003513:Cycloheximide / Q000494:pharmacology; D003594:Cytoplasmic Granules / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal / Q000187:drug effects; D005947:Glucose / Q000172:deficiency; D014176:Protein Biosynthesis / Q000187:drug effects; D020871:RNA Stability / Q000187:drug effects; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D013312:Stress, Physiological / Q000187:drug effects
chemical_list: D000596:Amino Acids; D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins; D003513:Cycloheximide; D005947:Glucose