Destruction and reconstitution of the dictyosome in the chrysophycean flagellate,Poterioochromonas malhamensis, after heat-shock, and other heat-shock effects

Schnepf, E.; Schmitt, U.

doi:10.1007/bf01275557

Cited by 8 publications

(1 citation statement)

References 25 publications

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“…These observations are strongly correlated with the inhibition of rRNA processing and ribosome assembly that is rapidly initiated after the beginning of HS (Arrigo et al, 1980;Neumann et al, 1984;Hadjiolov, 1985;Bell et al, 1988). Structural changes in the cytoplasm, mitochondrion, chloroplast, ER, and dictyosome have also been reported after HS (Heine et al, 1971;Skogqvist, 1974;Schnepf and Schmitt, 1981;Craig, 1985;Welch and Suhan, 1985).…”

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confidence: 68%

Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean

et al. 1997

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A monospecific polyclonal antibody was used to study the tissuetype specificity and intracellular localization of class I lowmolecular-weight (LMW) heat-shock proteins (HSPs) in soybean (Glycine max) under different heat-shock regimes. In etiolated soybean seedlings, the root meristematic regions contained the highest levels of LMW HSP. No tissue-type-specific expression of class I LMW HSP was detected using the tissue-printing method. In immunolocalization studies of seedlings treated with HS (40°C for 2 h) the class I LMW HSPs were found in the aggregated granular structures, which were distributed randomly in the cytoplasm and in the nucleus. When the heat shock was released, the granular structures disappeared and the class I LMW HSPs became distributed homogeneously in the cytoplasm. When the seedlings were then given a more severe heat shock following the initial 40°C + 28°C treatment, a large proportion of the class I LMW HSPs that originally localized in the cytoplasm were translocated into the nucleus and nucleolus. Class I LMW HSPs may assist in the resolubilization of proteins denatured or aggregated by heat and may also participate in the restoration of organellar function after heat shock.

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