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Protein synthesis by hybrid ribosomes reconstructed from rabbit reticulocyte ribosomal core-particles and amphibian or fungal split-proteins.
Cox RA
,
Greenwell P
.
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It was shown that high-salt (2.75 M-NH4Cl/69mM-MgCl2) shock treatment at 0 degrees C of the larger subparticles (L-subparticles) of rabbit, Xenopus laevis and Neurospora crassa cytoplasmic ribosomes yielded split-protein fractions that were not only functionally equivalent but also interchangeable. Thus, although the remaining core-particles were inactive in both the puromycin reaction and in poly(U)-directed polyphenylalanine synthesis, activity was restored when they were combined with either homologous or heterologous split-protein fractions. This technique was used to prepare active hybrid L-subparticles, e.g. rabbit cores/N. crassa split-proteins, and also active hybrid ribosomes, e.g. rabbit smaller subparticle/X. laevis core-particle/rabbit split-proteins. Rabbit and X. laevis split-protein fractions labelled with 14C by reductive methylation with [14C]formaldehyde and sodium cyanoborohydride were both shown to bind to rabbit core-particles in approximate correlation with the degree of re-activation. The split-protein fractions of rabbit and X. laevis L-subparticles were analysed by two-dimensional and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The molecular weights (measured in sodium dodecyl sulphate gels) of the split-proteins of rabbit and X. laevis L-subparticles were found to be similar. These results demonstrate that the peptidyltransferase active centre of cytoplasmic ribosomes of eukaryotes has components that are interchangeable over a wide evolutionary range. Evidently the essential molecular architecture of the active centre is highly conserved.
Arnstein,
The function of high-molecular-weight ribonucleic acid from rabbit reticulocytes in haemoglobin biosynthesis.
1964, Pubmed
Arnstein,
The function of high-molecular-weight ribonucleic acid from rabbit reticulocytes in haemoglobin biosynthesis.
1964,
Pubmed
Cammarano,
Formation of active hybrid 80-S particles from subunits of pea seedlings and mammalian liver ribosomes.
1972,
Pubmed
Cox,
Spectroscopic evidence for the uneven distribution of adenine and uracil residues in ribosomal ribonucleic acid of Drosophila melanogaster and of Plasmodium knowlesi and its possible evolutionary significance.
1976,
Pubmed
Cox,
A study of the influence of magnesium ions on the conformation of ribosomal ribonucleic acid and on the stability of the larger subribosomal particle of rabbit reticulocytes.
1976,
Pubmed
Cox,
Re-activation of the peptidyltransferase centre of rabbit reticulocyte ribosomes after inactivation by exposure to low concentrations of magnesium ion.
1976,
Pubmed
Cox,
Reassembly of the peptidyltransferase centre of larger subparticles of rabbit reticulocyte ribosomes from a core-particle and split-protein fraction.
1976,
Pubmed
Delaunay,
Evolution of ribosomal proteins.
1973,
Pubmed
Delaunay,
Evolution of ribosomal proteins.
1974,
Pubmed
Erdmann,
Structure and function of 5S and 5.8 S RNA.
1976,
Pubmed
Fischer,
Immunological comparison of the proteins of chicken and rat liver ribosomes.
1978,
Pubmed
Fricke,
Tritosol: a new scintillation cocktail based on Triton X-100.
1975,
Pubmed
Grasmuk,
Interchangeability of elongation factor-Tu and elongation factor-1 in aminoacyl-tRNA binding to 70 S and 80 S ribosomes.
1977,
Pubmed
Greenwell,
Affinity labelling of 23-S ribosomal RNA in the active centre of Escherichia coli peptidyl transferase.
1974,
Pubmed
Howard,
Ribosomal proteins from rabbit reticulocytes: number and molecular weights of proteins from ribosomal subunits.
1975,
Pubmed
Kaltschmidt,
Ribosomal proteins. VII. Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins.
1970,
Pubmed
Knopf,
A new two-dimensional gel electrophoresis system for the analysis of complex protein mixtures: application to the ribosome of E. coli.
1975,
Pubmed
Laemmli,
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
1970,
Pubmed
Lava-Sanchez,
Base composition of ribosomal RNA and evolution.
1972,
Pubmed
Littlechild,
A new method for the purification of 30S ribosomal proteins from Escherichia coli using nondenaturing conditions.
1978,
Pubmed
Martin,
Hybrid 80S monomers formed from subunits of ribosomes from protozoa, ungi, plants, and mammals.
1970,
Pubmed
Means,
Reductive alkylation of amino groups in proteins.
1968,
Pubmed
Moore,
Reductive methylation: a method for preparing functionally active radioactive ribosomes.
1973,
Pubmed
Noll,
Studies on proteins of animal ribosomes. 3. Immunochemical analyses of ribosomes from different tissues and species of animals.
1970,
Pubmed
Nomura,
Assembly of bacterial ribosomes.
1973,
Pubmed
Pace,
Homology of ribosomal ribonucleic acid diverse bacterial species with Escherichia coli and Bacillus stearothermophilus.
1971,
Pubmed
Pratt,
Dissociation of ribosomes from oocytes of Xenopus laevis into active subparticles.
1971,
Pubmed
,
Xenbase
Reboud,
Change of protein reactivity in mammalian ribosomal subunits as a function of temperature.
1977,
Pubmed
Rice,
Radioactive labeling of proteins in vitro.
1971,
Pubmed
Stöffler,
The identification of the eukaryotic ribosomal proteins homologous with Escherichia coli proteins L7 and L12.
1974,
Pubmed
Woese,
Conservation of primary structure in 16S ribosomal RNA.
1975,
Pubmed
