scholarly journals Nucleotide sequences of chloroplast 5S ribosomal ribonucleic acid in flowering plants

1979 ◽  
Vol 183 (3) ◽  
pp. 595-604 ◽  
Author(s):  
T A Dyer ◽  
C M Bowman
Keyword(s):  
Lemna Minor ◽  
Structural Features ◽  
Flowering Plants ◽  
5S Rrna ◽  
5S Rna ◽  
Homologous Sequences ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species ◽  
Strong Resemblance ◽  
Complete Digestion

Evidence for the sequence of duckweed (Lemna minor) chloroplast 5S rRNA was derived from the analysis of partial and complete enzymic digests of the 32P-labelled molecule. The possible sequence of the chloroplast 5S rRNA from three other flowering plants was deduced by complete digestion with T1 ribonuclease and comparison of the sequences of the oligonucleotide products with homologous sequences in the duckweed 5S rRNA. This analysis indicates that the chloroplast 5S rNA species differ appreciably from their cytosol counterparts but bear a strong resemblance to one another and to the 5S rRNA species of prokaryotes. Structural features apparently common to all 5S rRNA molecules are also discussed.

scholarly journals Nucleotide sequence analyses of the cytoplasmic 5S ribosomal ribonucleic acid from five species of flowering plants

1973 ◽  
Vol 135 (4) ◽  
pp. 845-851 ◽  
Author(s):  
P. I. Payne ◽  
M. J. Corry ◽  
T. A. Dyer
Keyword(s):  
Broad Bean ◽  
Flowering Plants ◽  
5S Rrna ◽  
Sequence Analyses ◽  
Two Dimensional Electrophoresis ◽  
Complementary Sequences ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species ◽  
Dimensional Electrophoresis ◽  
Dwarf Bean

Broad-bean 5S rRNA labelled with32P was digested separately with T1 and pancreatic A ribonucleases and the resulting oligonucleotides (20 and 18 respectively) were fractionated by two-dimensional electrophoresis. The oligonucleotides were analysed further and 32 of them have been completely sequenced. They were compared with those of 5S rRNA from dwarf bean, sunflower, tomato and rye. Sequence differences were found at both the 3′- and 5′-termini and at up to nine other positions. Most base substitutions were transitions between C and U. In common with other 5S rRNA species that have been analysed the ends of the molecule in each plant species have complementary sequences.

scholarly journals Higher-plant mitochondrial ribosomes contain a 5S ribosomal ribonucleic acid component

1976 ◽  
Vol 157 (1) ◽  
pp. 275-277 ◽  
Author(s):  
C J Leaver ◽  
M A Harmey
Keyword(s):  
Ribonucleic Acid ◽  
Plant Mitochondria ◽  
5S Rrna ◽  
Higher Plant ◽  
Acid Component ◽  
Mitochondrial Ribosomes ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species ◽  
Hydrogen Bonded

Ribosomes from higher-plant mitochondria contain 5S rRNA, in contrast with the mitochondrial ribosomes of animals and fungi, in which such a component has not been detected. In common with the ribosomes of prokaryotes and chloroplasts, higher-plant mitochondrial ribosomes do not appear to contain an RNA equivalent to the 5.8 S rRNA that is found in eukaryoytes hydrogen-bonded to the largest of the cytoplasmic rRNA species.

scholarly journals Identical 3′-terminal octanucleotide sequence in 18S ribosomal ribonucleic acid from different eukaryotes. A proposed role for this sequence in the recognition of terminator codons

1974 ◽  
Vol 141 (3) ◽  
pp. 609-615 ◽  
Author(s):  
John Shine ◽  
Lynn Dalgarno
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Drosophila Melanogaster ◽  
Ribosomal Rna ◽  
Ribonucleic Acid ◽  
18S Rrna ◽  
Base Sequence ◽  
Terminal Sequence ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species

The 3′-terminal sequence of 18S ribosomal RNA from Drosophila melanogaster and Saccharomyces cerevisiae was determined by stepwise degradation from the 3′-terminus and labelling with [3H]isoniazid. The sequence G-A-U-C-A-U-U-AOH was found at the 3′-terminus of both 18S rRNA species. Less extensive data for 18S RNA from a number of other eukaryotes are consistent with the same 3′-terminal sequence, and an identical sequence has previously been reported for the 3′-end of rabbit reticulocyte 18S rRNA (Hunt, 1970). These results suggest that the base sequence in this region is strongly conserved and may be identical in all eukaryotes. As the 3′-terminal hexanucleotide is complementary to eukaryotic terminator codons we discuss the possibility that the 3′-end of 18S rRNA may have a direct base-pairing role in the termination of protein synthesis.

The ribosomes of Plasmodium berghei: isolation and ribosomal ribonucleic acid analysis

Parasitology ◽  
1978 ◽  
Vol 77 (3) ◽  
pp. 345-366 ◽  
Author(s):  
F. W. Miller ◽  
Judith Ilan
Keyword(s):  
Plasmodium Berghei ◽  
Ribonucleic Acid ◽  
Ribosomal Subunit ◽  
High Yield ◽  
Small Component ◽  
40S Ribosomal Subunit ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species ◽  
Specific Degradation ◽  
Triton X

SummaryRibosomes and high molecular weight ribosomal ribonucleic acid (rRNA) from the blood stages of Plasmodium berghei parasites were studied in preparations free from host ribosome contamination. Purified malarial ribosomes were isolated in high yield from a population of ultrastructurally intact, viable parasites by hypertonic lysis with Triton X-100 and differential centrifugation. These ribosomes were shown to be derived from active polysomes and could be dissociated into subunits by puromycin–0·5 m KCl treatment. Malarial rRNA extracted from purified 40S and 60S ribosomal subunits was characterized by electrophoretic, sedimentation and base ratio analyses. Like certain other protozoa, the P. berghei 40S ribosomal subunit possessed an exceptionally large RNA species (mol. wt 0·9 × 106), while RNA isolated from the parasite's 60S subunit (mol. wt 1·5 × 106) was specifically ‘nicked’ to produce one large component (mol.wt 1·2 × 106) and one small component (mol.wt 0·3 × 106) in equimolar quantities. These rRNA's migrate identically on polyacrylamide gels after heating to 63°C for 5 mm or under denaturing conditions in the presence of formamide, indicating an absence of aggregation and non-specific degradation of the rRNA species. Base composition studies showed P. berghei rRNA to be low in guanosine and cytosine content, as is the case for protozoa generally.

Processing of eukaryotic pre-rRNA: the role of the transcribed spacers

1995 ◽  
Vol 73 (11-12) ◽  
pp. 789-801 ◽  
Author(s):  
Rob W. van Nues ◽  
Jaap Venema ◽  
Jeanette M. J. Rientjes ◽  
Anita Dirks-Mulder ◽  
Hendrik A. Raué
Keyword(s):  
Mutational Analysis ◽  
Structural Features ◽  
28S Rrna ◽  
Cis Acting ◽  
Processing Elements ◽  
Rrna Species ◽  
Polymerase I ◽  
Precursor Transcript

The 17–18S, 5.8S, and 25–28S rRNA species of eukaryotic cells are produced by a series of nucleolytic reactions that liberate the mature rRNAs from the large primary precursor transcript synthesized by RNA polymerase I. Whereas the order of the cleavage reactions has long been established, until recently little information was available on their molecular details, such as the nature of the proteins, including the nucleolytic enzymes, involved and the signals directing the processing machinery to the correct sites. This situation is now rapidly changing, in particular where yeast is concerned. The use of recently developed systems for in vivo mutational analysis of yeast rDNA has considerably enhanced our knowledge of cis-acting structural features within the pre-rRNA, in particular the transcribed spacer sequences, that are critical for correct and efficient removal of these spacers. The same systems also allow a link to be forged between trans-acting processing factors and these cis-acting elements. In this paper, we will focus predominantly on the nature and role of the cis-acting processing elements as identified in the transcribed spacer regions of Saccharomyces cerevisiae pre-rRNA.Key words: ribosome, processing, precursor rRNA, eukaryote, transcribed spacer.

scholarly journals Comparison of mammalian mitochondrial ribosomal ribonucleic acid from different species

1972 ◽  
Vol 128 (5) ◽  
pp. 1033-1041 ◽  
Author(s):  
R. S. Mitra ◽  
B. Bartoov ◽  
J. Monahan ◽  
K. B. Freeman
Keyword(s):  
Ionic Strength ◽  
Electrophoretic Mobility ◽  
Density Gradients ◽  
Molecular Weights ◽  
Mitochondrial Rrna ◽  
Electrophoretic Mobilities ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species ◽  
Low Ionic Strength ◽  
Human And Mouse

Mitochondrial ribosomal RNA species from mouse L cells, rat liver, rat hepatoma, hamster BHK-21 cells and human KB cells were examined by electrophoresis on polyacrylamide–agarose gels and sedimentation in sucrose density gradients. The SE (electrophoretic mobility) and S values of mitochondrial rRNA of all species were highly dependent on temperature and ionic strength of the medium; the SE values increased and the S values decreased with an increase in temperature at a low ionic strength. At an ionic strength of 0.3 at 23–25°C or an ionic strength of 0.01 at 3–4°C the S and SE values were almost the same being about 16.2–18.0 and 12.3–13.6 for human and mouse mitochondrial rRNA. The molecular weights under these conditions were calculated to be 3.8×105–4.3×105 and 5.9×105–6.8×105, depending on the technique used. At 25°C in buffers of low ionic strength mouse mitochondrial rRNA species had a lower electrophoretic mobility than those of human and hamster. Under these conditions the smaller mitochondrial rRNA species of hamster had a lower electrophoretic mobility than that of human but the larger component had an identical mobility. Mouse and rat mitochondrial rRNA species had identical electrophoretic mobilities. Complex differences between human and mouse mitochondrial rRNA species were observed on sedimentation in sucrose density gradients under various conditions of temperature and ionic strength. Mouse L-cell mitochondrial rRNA was eluted after cytoplasmic rRNA on a column of methylated albumin–kieselguhr.

A proposed nucleotide sequence for the 5S ribosomal ribonucleic acid of rainbow trout (Salmo gairdneri)

1978 ◽  
Vol 56 (1) ◽  
pp. 60-65 ◽  
Author(s):  
Kenneth L. Roy
Keyword(s):  
Rainbow Trout ◽  
Nucleotide Sequence ◽  
Ribonucleic Acid ◽  
Gel Electrophoresis ◽  
Inorganic Phosphate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Salmo Gairdneri ◽  
Ribosomal Ribonucleic Acid ◽  
Complete Digestion ◽  
Pancreatic Rnase

Rainbow trout cell cultures have been exposed to 32P-labelled inorganic phosphate and the labelled RNA has been isolated. The 5S ribosomal ribonucleic acid (5S rRNA) was purified by polyacrylamide gel electrophoresis, then digested with RNase T1 or pancreatic RNase. The products of complete digestion were separated and their sequences determined. These analyses have allowed a sequence to be proposed which differs in eight positions from that of mammalian 5S rRNAs.

scholarly journals A 5S rRNA/L5 complex is a precursor to ribosome assembly in mammalian cells.

1988 ◽  
Vol 106 (3) ◽  
pp. 545-556 ◽  
Author(s):  
J A Steitz ◽  
C Berg ◽  
J P Hendrick ◽  
H La Branche-Chabot ◽  
A Metspalu ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
5S Rrna ◽  
5S Rna ◽  
Rna Molecules ◽  
La Protein ◽  
Rnp Complex ◽  
Mouse Cells ◽  
Protein Moiety ◽  
Human And Mouse

A novel 5S RNA-protein (RNP) complex in human and mouse cells has been analyzed using patient autoantibodies. The RNP is small (approximately 7S) and contains most of the nonribosome-associated 5S RNA molecules in HeLa cells. The 5S RNA in the particle is matured at its 3' end, consistent with the results of in vivo pulse-chase experiments which indicate that this RNP represents a later step in 5S biogenesis than a previously described 5S*/La protein complex. The protein moiety of the 5S RNP has been identified as ribosomal protein L5, which is known to be released from ribosomes in a complex with 5S after various treatments of the 60S subunit. Indirect immunofluorescence indicates that the L5/5S complex is concentrated in the nucleolus. L5 may therefore play a role in delivering 5S rRNA to the nucleolus for assembly into ribosomes.

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