A cytoplasmic protein that promotes nucleo-cytoplasmic RNA transport in rat liver

1983 ◽  
Vol 11 (4) ◽  
pp. 371-371 ◽  
Author(s):  
ALEXANDER R. McDONALD ◽  
CHARLES A. STEWART ◽  
CHARLES D. GLEED ◽  
PAUL S. AGUTTER
Keyword(s):  
Rat Liver ◽  
Cytoplasmic Protein ◽  
Rna Transport ◽  
Cytoplasmic Rna

scholarly journals Ribosomal and informational ribonucleoprotein complexes of animal cells. Study on rat liver ribonucleic acids as constituents of ribonucleoprotein complexes by chromatography on nucleoprotein-celite columns.

1975 ◽  
Vol 147 (3) ◽  
pp. 447-456 ◽  
Author(s):  
A V Lichtenstein ◽  
R P Alechina ◽  
V S Shapot
Keyword(s):  
Rat Liver ◽  
Gradient Elution ◽  
Animal Cells ◽  
Ribonucleic Acids ◽  
Rna Molecules ◽  
Ribonucleoprotein Complexes ◽  
Cytoplasmic Rna ◽  
Novel Method ◽  
Gradual Release ◽  
Linear Concentration

A novel method of RNA fractionation has been developed. Nuclear and cytoplasmic rat liver RNA species were fractionated as constituents of corresponding ribonucleoprotein particles, which were previously adsorbed on a Celite-column by their protein component. The fractionation is based on a dissociation of the particles (linear concentration gradient of LiCl and urea with subsequent temperature gradient), which results in a gradual release of the RNA molecules from ribonucleoprotein complexes. Thus the fractionation is in accordance with the tightness of the RNA-protein bonds. A gradient elution of RNA from a nucleoprotein-Celite column permitted fractionation of both ribosomal and rapidly labelled non-ribosomal RNA. The latter, both nuclear and cytoplasmic, could be separated by chromatography on nucleoprotein-Celite columns into two main fractions (components I and V). In cytoplasmic RNA components I and V presumably correspond to mlRNA (messenger-like RNA of free cytoplasmic particles) and mRNA (template RNA associated with ribosomes) respectively.

Lack of major cytoplasmic protein contamination of rat liver nuclear chromatin

1972 ◽  
Vol 28 (5) ◽  
pp. 514-516 ◽  
Author(s):  
J. A. Wilhelm ◽  
Carlleen M. Groves ◽  
L. S. Hnilica
Keyword(s):  
Rat Liver ◽  
Nuclear Chromatin ◽  
Cytoplasmic Protein ◽  
Protein Contamination

SPECIFIC BINDING OF [3H]OESTRADIOL BY CYTOPLASMIC PROTEIN COMPONENTS OF FEMALE RAT LIVER

1976 ◽  
Vol 69 (1) ◽  
pp. 167-168 ◽  
Author(s):  
WENDY POWELL-JONES ◽  
PETER DAVIES ◽  
KEITH GRIFFITHS
Keyword(s):  
Rat Liver ◽  
Specific Binding ◽  
Female Rat ◽  
Cytoplasmic Protein ◽  
Protein Components

scholarly journals PTB/hnRNP I Is Required for RNP Remodeling during RNA Localization in Xenopus Oocytes

2007 ◽  
Vol 28 (2) ◽  
pp. 678-686 ◽  
Author(s):  
Raymond A. Lewis ◽  
James A. Gagnon ◽  
Kimberly L. Mowry
Keyword(s):  
Protein Interactions ◽  
Xenopus Oocytes ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Localization ◽  
Rna Transport ◽  
Rna Sequences ◽  
Cytoplasmic Rna ◽  
Embryonic Polarity ◽  
Specific Mrnas

ABSTRACT Transport of specific mRNAs to defined regions within the cell cytoplasm is a fundamental mechanism for regulating cell and developmental polarity. In the Xenopus oocyte, Vg1 RNA is transported to the vegetal cytoplasm, where localized expression of the encoded protein is critical for embryonic polarity. The Vg1 localization pathway is directed by interactions between key motifs within Vg1 RNA and protein factors recognizing those RNA sequences. We have investigated how RNA-protein interactions could be modulated to trigger distinct steps in the localization pathway and found that the Vg1 RNP is remodeled during cytoplasmic RNA transport. Our results implicate two RNA-binding proteins with key roles in Vg1 RNA localization, PTB/hnRNP I and Vg1RBP/vera, in this process. We show that PTB/hnRNP I is required for remodeling of the interaction between Vg1 RNA and Vg1RBP/vera. Critically, mutations that block this remodeling event also eliminate vegetal localization of the RNA, suggesting that RNP remodeling is required for localization.

scholarly journals The effect of dietary protein deficiency on albumin synthesis and on the concentration of active albumin messenger ribonucleic acid in rat liver

1978 ◽  
Vol 172 (1) ◽  
pp. 129-135 ◽  
Author(s):  
V M Pain ◽  
M J Clemens ◽  
P J Garlick
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Dietary Protein ◽  
Liver Protein ◽  
Albumin Synthesis ◽  
Deficient Diet ◽  
Messenger Ribonucleic Acid ◽  
Cytoplasmic Rna ◽  
Reticulocyte Lysate ◽  
Albumin Mrna

In rats fed on a protein-deficient diet, albumin synthesis as a percentage of total liver protein synthesis falls from the normal value of approx. 15% to about 8%. We have extracted total cytoplasmic RNA from individual rat livers and measured the concentration of active albumin mRNA by translation in a reticulocyte lysate system from which the endogenous mRNA had been removed [Pelham & Jackson (1976) Eur. J. Biochem. 67, 247-256]. In this messenger-dependent system it is possible to measure the synthesis of albumin as a proportion of the overall protein synthesis promoted by the addition of the hepatic RNA. The results show that the concentration of translatable albumin mRNA in samples of total cytoplasmic RNA from livers of protein-deficient rats is decreased markedly. These findings suggest that dietary protein supply affects selectively the synthesis and/or functional stability of albumin mRNA in rat liver.

scholarly journals Importance of mammalian nuclear-envelope nucleoside triphosphatase in nucleo-cytoplasmic transport of ribonucleoproteins

1979 ◽  
Vol 182 (3) ◽  
pp. 811-819 ◽  
Author(s):  
P S Agutter ◽  
B McCaldin ◽  
H J McArdle
Keyword(s):  
Ionic Strength ◽  
Substrate Specificity ◽  
Nuclear Envelope ◽  
Nucleoside Triphosphate ◽  
Rna Transport ◽  
Isolated Nuclei ◽  
Cytoplasmic Rna ◽  
Cytoplasmic Transport ◽  
Nucleoside Triphosphatase

The nucleoside triphosphate-stimulated efflux of RNA from isolated nuclei was studied under a range of conditions, and the effects of these conditions on the process were compared with the properties of the nucleoside triphosphatase located in the pore complex. A marked similarity between the rate of efflux and the rate of nucleoside triphosphate hydrolysis was apparent, in terms of substrate specificity, sensitivity to treatment with insolubilized trypsin, kinetics and the effects of increased ionic strength and of many inhibitors. These results are taken, in view of earlier evidence, to suggest that the activity of the nucleoside triphosphatase is a prerequisite for nucleo-cytoplasmic RNA transport in vivo. There are some indications that the nuclear-envelope lipid is also involved in regulating the efflux process.

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