A Hybrid-Body Containing Constituents of Both P-Bodies and Stress Granules Forms in Response to Hypoosmotic Stress in Saccharomyces cerevisiae

• Published in: PloS one Vol. 11; no. 6; p. e0158776
• Main Authors: Shah, Khyati H, Varia, Sapna N, Cook, Laura A, Herman, Paul K
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 30-06-2016; Public Library of Science (PLoS)
• Subjects: Baking yeast; Biology and Life Sciences; Cell cycle; Cytoplasm; Cytoplasm - metabolism; Cytoplasmic Granules - metabolism; Environmental effects; Experiments; Glucose; Granular materials; Kinases; Molecular biology; Organelles; Physical Sciences; Proteins; Research and Analysis Methods; Ribonucleoproteins - metabolism; Saccharomyces cerevisiae; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - metabolism; Signal transduction; Stress; Stress, Physiological - physiology; Stresses; Yeast; United States > US; Ohio
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0158776

The cytoplasm of the eukaryotic cell is a highly compartmentalized space that contains a variety of ribonucleoprotein (RNP) granules in addition to its complement of membrane-bound organelles. These RNP granules contain specific sets of proteins and mRNAs and form in response to particular environmental and developmental stimuli. Two of the better-characterized of these RNP structures are the stress granule and Processing-body (P-body) that have been conserved from yeast to humans. In this report, we examined the cues regulating stress granule assembly and the relationship between stress granule and P-body foci. These two RNP structures are generally thought to be independent entities in eukaryotic cells. However, we found here that stress granule and P-body proteins were localized to a common or merged granule specifically in response to a hypoosmotic stress. Interestingly, these hybrid-bodies were found to be transient structures that were resolved with time into separate P-body and stress granule foci. In all, these data suggest that the identity of an RNP granule is not absolute and that it can vary depending upon the nature of the induction conditions. Since the activities of a granule are likely influenced by its protein constituency, these observations are consistent with the possibility of RNP granules having distinct functions in different cellular contexts.