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PMID: 2410257 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The EMBO journal ·Vol. 4 ·No. 2 ·1985-02-00 ·Pages 399-406

Arrigo AP, Darlix JL, Khandjian EW, Simon M, Spahr PF

Abstract

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.

MeSH Terms
Animals Base Sequence Cell Compartmentation Cytoplasm/ultrastructure Drosophila melanogaster/physiology,ultrastructure Heat-Shock Proteins/immunology,metabolism Hot Temperature Isoelectric Point Macromolecular Substances Microscopy, Electron Molecular Weight RNA/analysis RNA, Small Nuclear Ribonucleoproteins/analysis,metabolism
Chemicals
Heat-Shock Proteins Macromolecular Substances RNA, Small Nuclear Ribonucleoproteins RNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Arrigo A P
Darlix J L
Khandjian E W
Simon M
Spahr P F
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1985-02-00
Pages
399-406
Language
English
Region
England
NLM ID
8208664
PMCID
PMC554199
Subset
IM
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