The Journal of Cell Biology, Vol 106, 1131-1139, Copyright © 1988 by The Rockefeller University Press

ARTICLES

Ultrastructural and biochemical analysis of the stress granule in chicken embryo fibroblasts

NC Collier, J Heuser, MA Levy and MJ Schlesinger
Department of Microbiology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110.

The ultrastructure and biochemical composition of cytoplasmic particles that form in chicken embryo fibroblasts during stress have been analyzed. We showed previously that these particles contained the small stress protein, sp 24, and antibodies specific to sp 24 were used here to identify the stress granule. In thin sections, the stress granule was a densely staining, membraneless, cytoplasmic body and appeared as a highly condensed area of cytoplasm in freeze-fracture preparations. Hypotonic swelling of cells before freeze-fracture analysis revealed a basketlike structure composed of interconnecting protein cables. No other proteins could be cross-linked to sp 24 when stress granules were treated with dithiobis-(succinimidyl propionate). High resolution autoradiographic analysis with [3H]uridine failed to identify any associated RNA synthesized in the period immediately before the stress. Thus the stress granule appears to be composed predominantly of sp 24 aggregates. Sp 24 could be purified to homogeneity from the stress granule by solubilization in 8 M urea and anion exchange chromatography.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

• Sukarieh, R., Sonenberg, N., Pelletier, J. (2009). The eIF4E-binding proteins are modifiers of cytoplasmic eIF4E relocalization during the heat shock response. Am. J. Physiol. Cell Physiol. 296: C1207-C1217 [Abstract] [Full Text]  
• Dimberg, A., Rylova, S., Dieterich, L. C., Olsson, A.-K., Schiller, P., Wikner, C., Bohman, S., Botling, J., Lukinius, A., Wawrousek, E. F., Claesson-Welsh, L. (2008). {alpha}B-crystallin promotes tumor angiogenesis by increasing vascular survival during tube morphogenesis. Blood 111: 2015-2023 [Abstract] [Full Text]  
• Basha, E., Lee, G. J., Breci, L. A., Hausrath, A. C., Buan, N. R., Giese, K. C., Vierling, E. (2004). The Identity of Proteins Associated with a Small Heat Shock Protein during Heat Stress in Vivo Indicates That These Chaperones Protect a Wide Range of Cellular Functions. J. Biol. Chem. 279: 7566-7575 [Abstract] [Full Text]  
• Mazroui, R., Huot, M.-E., Tremblay, S., Filion, C., Labelle, Y., Khandjian, E. W. (2002). Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression. Hum Mol Genet 11: 3007-3017 [Abstract] [Full Text]  
• Anderson, P., Kedersha, N. (2002). Stressful initiations. J. Cell Sci. 115: 3227-3234 [Abstract] [Full Text]  
• Kedersha, N. L., Gupta, M., Li, W., Miller, I., Anderson, P. (1999). RNA-Binding Proteins Tia-1 and Tiar Link the Phosphorylation of Eif-2{alpha} to the Assembly of Mammalian Stress Granules. JCB 147: 1431-1442 [Abstract] [Full Text]  
• Ehrnsperger, M., Lilie, H., Gaestel, M., Buchner, J. (1999). The Dynamics of Hsp25 Quaternary Structure. STRUCTURE AND FUNCTION OF DIFFERENT OLIGOMERIC SPECIES. J. Biol. Chem. 274: 14867-14874 [Abstract] [Full Text]  
• Beresford, P. J., Jaju, M., Friedman, R. S., Yoon, M. J., Lieberman, J. (1998). A Role for Heat Shock Protein 27 in CTL-Mediated Cell Death. J. Immunol. 161: 161-167 [Abstract] [Full Text]  
• Wotton, D., Freeman, K., Shore, D. (1996). Multimerization of Hsp42p, a Novel Heat Shock Protein of Saccharomyces cerevisiae, Is Dependent on a Conserved Carboxyl-terminal Sequence. J. Biol. Chem. 271: 2717-2723 [Abstract] [Full Text]  
• Sauk, J. J. (1990). Stress Proteins in Development And Disease. CROBM 1: 235-245 [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents