TY - JOUR
T1 - Isolation and visualization of large compact ribonucleoprotein particles of specific nuclear RNAs
AU - Spann, P.
AU - Feinerman, M.
AU - Sperling, J.
AU - Sperling, R.
PY - 1989
Y1 - 1989
N2 - 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 β-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 secretion of ~ 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.
AB - 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 β-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 secretion of ~ 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.
UR - http://www.scopus.com/inward/record.url?scp=0024509154&partnerID=8YFLogxK
U2 - 10.1073/pnas.86.2.466
DO - 10.1073/pnas.86.2.466
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C2 - 2521390
AN - SCOPUS:0024509154
SN - 0027-8424
VL - 86
SP - 466
EP - 470
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 2
ER -