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PubMed1980

Developmental changes in the molecular weight of heterogeneous nuclear RNA.

The size distribution of heterogeneous nuclear RNA (hnRNA) in the sea urchin embryo changes markedly during early development. Measurement of cleavage (4.5 h) to late gastrula (40 h) hnRNA by sedimentation in aqueous and denaturing solvent indicates that in the stages tested cleavage (4.5 h) hnRNA is smallest and rotating blastula (13 h) hnRNA is largest. The molecular weight of cleavage hnRNA is calculated to be about one-third that of rotating blastula hnRNA. Sedimentation of early embryo hnRNA in denaturing solvent to disaggregate complexes demonstrated mean S values lower than those obtained in aqueous solvent.

Animals↗
PubMed1979

Effect of 5-bromodeoxyuridine on heterogeneous nuclear RNA in rat hepatoma cells.

Heterogeneous nuclear RNA HnRNA) was isolated from untreated and 5-bromodeoxyuridine (BrdUrd) treated hepatoma tissue culture (HTC) cells. analysis of this RNA by either electrophoresis on polyacrylamide-agarose gels or centrifugation in sucrose gradients demonstrated that BrdUrd caused a shift in the labeled HnRNA population toward a smaller size distribution. This effect was produced by concentrations of BrdUrd which specifically lower the level of the differentiated enzyme tyrosine aminotransferase, but do not greatly affect cell growth. Differential binding to oligo(dT) cellulose was used to fractionate HnRNA further into classes containing poly(A) (alpha), oligo(A) (beta) or neither category of A-rich sequences (gamma). BrdUrd did not alter the relative rates of uridine incorporation into the three classes. The shift in the labeled HnRNA population due to BrdUrd was observed in all three subclasses of HnRNA.

Animals↗
PubMed1981

Structure of nuclear ribonucleoprotein: identification of proteins in contact with poly(A)+ heterogeneous nuclear RNA in living HeLa cells.

The processing of heterogeneous nuclear RNA into messenger RNA takes place in special nuclear ribonucleoprotein particles known as hnRNP. We report here the identification of proteins tightly complexed with poly(A)+ hnRNA in intact HeLa cells, as revealed by a novel in situ RNA-protein cross-linking technique. The set of cross-linked proteins includes the A, B, and C "core" hnRNP proteins, as well as the greater than 42,000 mol wt species previously identified in noncross-linked hnRNP. These proteins are shown to be cross-linked by virtue of remaining bound to the poly(A)+ hnRNA in the presence of 0.5% sodium dodecyl sulfate, 0.5 M NaCl, and 60% formamide, during subsequent oligo(dT)-cellulose chromatography, and in isopycnic banding in Cs2SO4 density gradients. These results establish that poly(A)+ hnRNA is in direct contact with a moderately complex set of nuclear proteins in vivo. This not only eliminates earlier models of hnRNP structure that were based upon the concept of a single protein component but also suggests that these proteins actively participate in modulating hnRNA structure and processing in the cell.

Centrifugation, Isopycnic↗
PubMed1970

A comparison between heterogeneous nuclear RNA and polysomal messenger RNA in HeLa cells by RNA-DNA hybridization.

Heterogeneous nuclear RNA (HnRNA) and mRNA from cytoplasmic polyribosomes of HeLa cells have been compared by RNA-DNA hybridization tests. 1 microg of HeLa cell DNA binds 0.05-0.10 microg of either HnRNA or mRNA. In addition, HeLa DNA that is preexposed to unlabeled HnRNA was found to have a reduced capacity to bind either HnRNA or mRNA. The results are compatible with considerable sequence similarity in the two types of RNA but, as is discussed, firm conclusions are precluded by imperfections of the hybridization reaction as presently employed.

Cell Nucleus↗
PubMedDate not supplied

Heterogeneous nuclear RNA from hairy cell leukemia patients activates 2',5'-oligoadenylate synthetase.

Interferon treatment of cells induces double-stranded RNA (dsRNA)-dependent 2',5' oligoadenylate (2-5A) synthetase, an enzyme which has been implicated in the mechanism of growth arrest in tumour cells. Since interferon (IFN) can inhibit the growth of cells that are not infected with virus, natural non-viral dsRNAs should be present in these cells which can activate 2-5A synthetase. If such nuclear dsRNAs are associated with the mechanism of growth control, cells inherently sensitive to growth inhibition by IFN should contain significant levels of 2-5A synthetase-activating dsRNAs. We measured the ability of size fractionated nuclear dsRNAs isolated from patients with hairy cell leukemia (HCL) to activate purified 2-5A synthetase. Peripheral blood mononuclear cells from HCL patients were utilized because of the inherent sensitivity of these patients to IFN treatment. The heterogeneous nuclear RNA fraction from four out of five HCL patients showed high levels of 2-5A synthetase-activating dsRNAs. The 2-5A formed contained biologically active trimers, tetramers, pentamers and hexamers as demonstrated by HPLC analysis and their ability to activate RNase L. In contrast, the nuclear RNA fraction from three out of four healthy controls were unable to activate 2-5A synthetase. These results indicate that natural, nuclear dsRNAs inherently exist in IFN-sensitive cells and imply that these molecules may play a role in the inhibition of cellular growth.

2',5'-Oligoadenylate Synthetase↗
PubMed1977

Heterogeneous nuclear RNA secondary structure: oligo (U) sequences base-paired with poly (A) and their possible role as binding sites for heterogeneous nuclear RNA-specific proteins.

HeLa cell heterogeneous nuclear RNA derived from high-molecular-weight nuclear ribonucleoprotein (RNP) particles contains oligo(U) sequences of 15-50 nucleotides base-paired with poly(A). These duplexes are resistant to pancreatic RNase at 0.5 M NaCl in native RNP, remain so after chemical deproteinization of the RNP digests, and then copurify with poly(A) on oligo(dT)-cellulose chromatography. Oligo(dT)-cellulose binding capacity of the oligo(U)-poly(A) duplexes is abolished by prior titration of the nonduplex poly(A) regions with excess poly(U). The oligo(dT)-purified fraction is 97.5 mole % A + U and the [3H]uridine-labeled component is resistant to redigestion by pancreatic RNase at 0.5 M NaCl but not at 0.01 M NaCl. After thermal denaturation, the [3H]uridine-labeled chains become RNase-sensitive at 0.5 M NaCl. Electrophoresis of [3H]adenosine- or [3H]uridine-labeled material in polyacrylamide gels containing 99% formamide confirms that the oligo(U) sequences are not covalently linked to poly(A). Controls establish that the A-U duplexes are not formed artifactually during isolation of heterogeneous nuclear RNP or subsequent fractionation. The oligo(U)-poly(A) duplexes appear to be associated with protein in native heterogeneous nuclear RNP, as reflected by the differential pancreatic RNase sensitivity of the duplexed oligo(U) in RNP (resistant) and RNA (sensitive), measured at physiological ionic strength.

Base Sequence↗
PubMed1978

Proteins bound to heterogeneous nuclear RNA of simian-virus-40-infected cells.

Heterogeneous nuclear RNA . protein (hnRNA . protein) complexes from simian-virus-40 (SV40)-infected cells late in infection contain 7--10% RNA sequences specific to SV40 DNA. The SV40 nuclear RNA . protein complexes sediment at 60--70 S. The reality and specificity of the RNA-protein association is shown in metrizamide gradients. Protein and RNA lebels of hnRNA . protein-particles in SV40-infected cells follow a parallel pattern with a peak at 1.28 g/cm2 whereas a mixture of ribosomal RNA and soluble cytoplasmic proteins is separated according to the different densities in metrizamide. Analysis of hnRNA . protein from infected cells by two-dimensional gel electrophoresis shows the presence of a number of new proteins. It is demonstrated that three of these proteins are cellular ones induced by the virus infection and hence constitute good candidates to be specific RNA . protein particles for virus nuclear RNA. The presence of actin in hnRNA . protein particles from normal and SV40-infected cells and the presence of the major capsid protein VP1 in hnRNA . protein particles from SV40-infected cells is discussed.

Base Sequence↗
PubMed1979

Properties of a small transcribed poly A sequence in heterogeneous nuclear RNA of HeLa cells.

A class of heterogeneous nuclear RNA (hnRNA) molecules contain an internal transcribed poly A sequence of close to 25 uninterrupted AMP residues. HnRNA molecules containing this sequence are separable from those containing the large 3' terminal poly A sequence on the basis of their differential affinity for oligo dT cellulose. The fact that the transcribed small poly A and the 3' terminal poly A are not found in the same hnRNA molecules even though both are present in similar size classes and that the small poly A is absent from cytoplasmic messenger RNA (mRNA) has led us to propose a scheme for mRNA processing in which the 3' end of the small poly A in hnRNA becomes a priming size for the post-transcriptional addiction of the large poly A.

HeLa Cells↗
PubMed1977

Secondary structure of heterogeneous nuclear RNA: two classes of double-stranded RNA in native ribonucleoprotein.

Heterogeneous nuclear RNA (hnRNA) from HeLa cells contains intramolecular duplexes. Since hnRNA is associated with protein in vivo, it is possible that the double-stranded regions observed in deproteinized hnRNA form spontaneously upon the release of protein from single-stranded but potentially complementary sequences. We show here that this is not the case for a class of double-stranded sequences that is defined by resistance to RNases A + T(1) at high ionic strength. Exposure of HeLa hnRNA.ribonucleoprotein (hnRNP) particles to Escherichia coli RNase III, a double-strand-specific endoribonuclease, destroys most of the sequences resistant to RNases A + T(1). This effect is completely blocked when hnRNP is exposed to RNase III in the presence of an excess of purified double-stranded RNA. In addition, we show that there exist two classes of double-stranded RNA in hnRNP at a salt concentration of 0.13 M. These are distinguished by their relative resistance to RNases A + T(1). The more stable double-stranded sequences, which are resistant to RNases A + T(1) at 0.13 M, comprise 1.0-1.1% of the nucleotides in hnRNP. The less stable double-stranded sequences comprise an additional 1.5-2.0% of the nucleotides in hnRNP. These are sensitive to RNase III at 0.13 M, but are not resistant to RNases A + T(1) unless the salt concentration is raised to 0.63 M. The demonstration that double-stranded sequences resistant to RNases A + T(1) exist in native ribonucleoprotein and are not artifacts of deproteinization now makes it appropriate to seriously consider their possible functional role in hnRNA metabolism, perhaps as binding sites for regulatory proteins involved in mRNA processing.

Cell Nucleus↗
PubMed1977

Preparation in undenatured form of the main protein bound to heterogeneous nuclear RNA in liver and hepatoma cells.

Particles carrying heterogeneous nuclear RNA (30 S-particles) were prepared from rat liver and Zajdela hepatoma ascites cell nuclei after ultrasonic disruption. The ribonucleoprotein structures were disintegrated in the presence of 100mM spermidine. Using chromatography on Sepharose-polyadenylate a protein component has been obtained which possessed high affinity for heterogeneous nuclear RNA, polyuridylate and polyadenylate, and double-stranded DNA. This protein was the main species of the ribonucleoprotein studied; it showed bands with molcular weights of 37000 and 40000 respectively in SDS gel electrophoresis. The RNA-binding proteins isolated from liver and hepatoma had identical molecular weights and the same affinity for Sepharose-polyadenylate used in the isolation.

Animals↗
PubMed1982

Heterogeneous nuclear RNA promotes synthesis of (2',5')oligoadenylate and is cleaved by the (2',5')oligoadenylate-activated endoribonuclease.

Heterogeneous nuclear RNA contains double-stranded regions that are not found in mRNA and that may serve as recognition elements for processing enzymes. The double-stranded regions of heterogeneous nuclear RNA prepared from HeLa cells promoted the synthesis of (2',5')oligoadenylate [(2',5')oligo(A) or (2'5')An] when incubated with (2',5')An polymerase. This enzyme is present in elevated levels in interferon-treated cells, and labeled heterogeneous nuclear RNA incubated with extracts of these cells is preferentially cleaved, since mRNA included in the same incubations is not appreciably degraded. The cleavage of heterogenous nuclear RNA is caused by the synthesis of (2'5')An and by a "localized" activation of the (2',5')An-dependent endonuclease, since it was enhanced by ATP, the substrate of the (2',5')An polymerase, and inhibited by 2'-dATP and ethidium bromide. Both of these compounds suppress the synthesis of (2',5')An, the first by competitive inhibition and the latter by intercalating into double-stranded RNA. The possible role of double-stranded regions and of the (2',5')An polymerase-endonuclease system in the processing of heterogeneous nuclear RNA is discussed.

2',5'-Oligoadenylate Synthetase↗
PubMed1984

Base-specific ribonucleases potentially involved in heterogeneous nuclear RNA processing and poly(A) metabolism.

Polyadenylation and splicing of heterogeneous nuclear RNA, two crucial steps in mRNA processing, are apparently enzymatically mediated processes. This contribution summarizes the properties and the presumed functions of the known poly(A) catabolic enzymes (endoribonuclease IV and V, 2',3'- exoribonuclease ) as well as those of the pyrimidine-specific endoribonucleases associated with snRNP -hnRNP complexes (endoribonuclease VII, acidic pI 4.1 endoribonuclease and poly(U)-specific U1 snRNP -nuclease).

Animals↗
PubMed1979

Kinetics of hybridization to human DNA of heterogeneous nuclear RNA isolated from normal human lymphoblasts and acute leukemia blast cells.

Heterogeneous nuclear RNA was extracted from normal PHA-stimulated human lymphocytes and acute myeloid leukemia blast cells. Experiments were performed to determine the hybridization kinetics of these RNA's to human DNA. The best least squares solutions indicate in the hybridization reaction of both normal and leukemic RNA two main components. For leukemic cell RNA the rate constants of both components were significantly different from that of normal cell RNA. In particular, the difference between the rate constants of the second lower component suggests that the slowly hybridizing sequences in leukemic cell RNA have a degree of repetition higher than of the corresponding sequences of normal cell RNA.

Base Sequence↗
PubMed1975

Ribosome-dependent conversion of polyA-containing heterogenous nuclear RNA into smaller RNA molecules.

The polyA-containing heterogenous nuclear RNA fraction separated from total rat liver nRNA by gel filtration on Sepharose 4B followed by affinity chromatography on polyU-Sepharose and containing predominantly the 45S components becomes enzymatically bound to homologous 80S ribosomes and polyribosomes at 0 degree C. If 80S ribosomes or polyribosomes with bound poly-a-containing HnRNA are subjected to a further incubation at 37 degree C, the original 45S RNA is gradually converted into smaller RNA species of 10- 35S which remain bound to the particle. This ribosome-dependent cleavage of larger HnRNA species into smaller RNA molecules may represent the ultimate step of mRNA maturation.

Adenine Nucleotides↗
PubMed1979

Two-dimensional analysis of proteins associated with heterogenous nuclear RNA in various animal cell lines.

The protein complement of heterogenous nuclear RNA . protein particles from human HeLA, mouse L and Chinese hamster (CHO) cells has been analysed by two-dimensional gel electrophoresis using the two techniques described by O'Farrell [J. Biol. Chem. (1975) 250, 4007--4021 and Cell (1977) 12, 1133--1142]. Over a hundred individual spots habe been reproducibly detected both L-[35S]methionine. Large similarities, especially in the 25 000--40 000 Mr cluster of basic protein, were found among these three mammalian species. As far as phosphoproteins are concerned, it was observed that the bands already described by one-dimensional gels [Eur. J. Biochem. (1978) 86, 301--310] with Mr values of 28 000, 30 000, 37 000 and 52 000 are resolved into about 15 individual spots, suggesting a corresponding number of distinct states of phosphorylation. It was also clearly demonstrated that phosphoproteins are unrelated to the major basic protein species. Particles of different size classes were analysed with respect to their content of individual proteins, both non-phosphorylated and phosphorylated. The most salient feature observed was that phosphoproteins become progressively more abundant with particles of increasing size. This raises the possibility that at least some of these phosphoproteins might belong to a nuclear structure to which hnRNA is normally bound.

Animals↗