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. 1989 Mar;9(3):1298–1308. doi: 10.1128/mcb.9.3.1298

Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs.

L Nover 1, K D Scharf 1, D Neumann 1
PMCID: PMC362722  PMID: 2725500

Abstract

In heat-shocked tomato cell cultures, cytoplasmic heat shock granules (HSGs) are tightly associated with a specific subset of mRNAs coding mainly for the untranslated control proteins. This messenger ribonucleoprotein complex was banded in a CsCl gradient after fixation with formaldehyde (approximately 1.30 g/cm3). It contains all the heat shock proteins and most of the RNA applied to the gradient. During heat shock, a reversible aggregation of HSGs from 15S precursor particles can be shown. These pre-HSGs are not identical to the 19S plant prosomes. Ultrastructural analysis supports the ribonucleoprotein nature of HSGs and their composition of approximately 10-nm precursor particles. A model summarizes our results. It gives a reasonable explanation for the striking conservation of untranslated mRNAs during heat shock and may apply also to animal cells.

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Selected References

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