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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1989 Jan;86(2):466–470. doi: 10.1073/pnas.86.2.466

Isolation and visualization of large compact ribonucleoprotein particles of specific nuclear RNAs.

P Spann 1, M Feinerman 1, J Sperling 1, R Sperling 1
PMCID: PMC286491  PMID: 2521390

Abstract

We have previously shown that nuclear transcripts of the multifunctional enzyme, carbamoyl-phosphate synthetase, aspartate transcarbamylase, dihydroorotase RNA can be released from nuclei of Syrian hamster cells as compact ribonucleoprotein (RNP) particles that sediment at the 200S region in a sucrose gradient. The 200S nuclear RNP particles contain U1, U2, and U6 small nuclear RNPs, which are known to be required for splicing of pre-mRNA, as integral components of the particles. In this study we demonstrate that nuclear transcripts of dihydrofolate reductase in Syrian hamster cells and of beta-actin in both Syrian hamster and human cells are also released from the respective nuclei as 200S particles--despite the difference in length of these RNAs. Electron microscopy of the 200S particles revealed discrete compact composite structures with a cross section of approximately 50 nm. Finding that two more nuclear RNAs from two different cell types and two different species are released as 200S RNP particles suggests a general mode for packaging of heterogeneous nuclear RNA in large compact RNP particles the size of which is independent of the RNA length.

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Selected References

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