Scientific article

Characterization of the prosome from Drosophila and its similarity to the cytoplasmic structures formed by the low molecular weight heat-shock proteins

Published inEMBO Journal, vol. 4, no. 2, p. 399-406
Publication date1985

We have identified and characterized a ribonucleoprotein structure from the cytoplasm of Drosophila melanogaster tissue culture cells which is equivalent to the prosome, a recently described ribonucleoprotein particle of duck and mouse cells. During the recovery period following heat shock, the low mol. wt. heat-shock proteins form cytoplasmic ribonucleoprotein particles which co-purify with the Drosophila prosome. Both ribonucleoprotein particles share several structural properties but their protein constituents differ in their metabolism and cellular localization during the heat treatment. We also report the partial nucleotide sequences of several small RNA species associated with the Drosophila prosome. One of them has a strong sequence homology with the U6 mammalian small nuclear RNA.

  • Animals
  • Base sequence
  • Cell compartmentation
  • Cytoplasm/ultrastructure
  • Drosophila melanogaster/physiology/ultrastructure
  • Heat-shock proteins/immunology/metabolism
  • Hot temperature
  • Isoelectric point
  • Macromolecular substances
  • Electron microscopy
  • Molecular weight
  • RNA/analysis
  • Small nuclear RNA
  • Ribonucleoproteins/analysis/metabolism
  • Swiss National Science Foundation - 3.321.82
  • Swiss National Science Foundation - 3.567.83
Citation (ISO format)
ARRIGO, André-Patrick et al. Characterization of the prosome from <i>Drosophila</i> and its similarity to the cytoplasmic structures formed by the low molecular weight heat-shock proteins. In: EMBO Journal, 1985, vol. 4, n° 2, p. 399–406.
Main files (1)
Article (Published version)
ISSN of the journal0261-4189

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