phosphorus-radioisotopes and alpha-sarcin

phosphorus-radioisotopes has been researched along with alpha-sarcin* in 2 studies

Other Studies

2 other study(ies) available for phosphorus-radioisotopes and alpha-sarcin

Article	Year
Placement of the alpha-sarcin loop within the 50S subunit: evidence derived using a photolabile oligodeoxynucleotide probe. Nucleic acids research, 1997, Nov-15, Volume: 25, Issue:22 We report the synthesis of a radioactive, photolabile oligodeoxyribonucleotide probe and its exploitation in identifying 50S ribosomal subunit components neighboring the alpha-sarcin loop. The probe is complementary to 23S rRNA nt 2653-2674. Photolysis of the complex formed between the probe and 50S subunits leads to site-specific probe photoincorporation into proteins L2, the most highly labeled protein, L1, L15, L16 and L27, labeled to intermediate extents, and L5, L9, L17 and L24, each labeled to a minor extent. Portions of each of these proteins thus lie within 23 A of nt U2653. These results lead us to conclude that the alpha-sarcin loop is located at the base of the L1 projection within the 50S subunit. Such placement, near the peptidyl transferase center, provides a rationale for the extreme sensitivity of ribosomal function to cleavage of the alpha-sarcin loop. Topics: Affinity Labels; Azides; Binding Sites; DNA, Complementary; Endoribonucleases; Fungal Proteins; Genetic Complementation Test; Isotope Labeling; Nucleic Acid Conformation; Oligonucleotide Probes; Phosphorus Radioisotopes; RNA, Ribosomal; RNA, Ribosomal, 23S	1997
RNA present in post-ribosomal supernatants makes ribosomes susceptible to inactivation by gelonin and alpha-sarcin. Biochemistry and molecular biology international, 1994, Volume: 32, Issue:3 The remarkable resistance of isolated ribosomes to gelonin is overcome by cofactors present in post-ribosomal supernatants. In rat liver post-ribosomal supernatant RNA is the cofactor responsible of the sensitization of ribosomes. Isolated RNA, which consists mostly of deacylated tRNA, accounts for less than 10 per cent of the activity of the original supernatant. The activity of the supernatant is completely destroyed by micrococcal nuclease and RNAase A and also by proteinase K, suggesting that some protein enhances the effect of RNA. RNA has a role also in the sensitization of ribosomes to alpha-sarcin, an RNAase which inactivates ribosomes by hydrolyzing a single phosphodiester bond in the same region of 28S rRNA which is the target of the N-glycosidase activity of gelonin. Topics: Animals; Artemia; Autoradiography; Cytosol; Electrophoresis, Polyacrylamide Gel; Endopeptidase K; Endoribonucleases; Fungal Proteins; Liver; Molecular Weight; Phosphorus Radioisotopes; Plant Proteins; Protein Synthesis Inhibitors; Rabbits; Rats; Reticulocytes; Ribonuclease, Pancreatic; Ribosome Inactivating Proteins, Type 1; Ribosomes; RNA; RNA, Ribosomal; RNA, Ribosomal, 28S; RNA, Transfer; Serine Endopeptidases	1994

Article

Year

Placement of the alpha-sarcin loop within the 50S subunit: evidence derived using a photolabile oligodeoxynucleotide probe.

Nucleic acids research, 1997, Nov-15, Volume: 25, Issue:22

We report the synthesis of a radioactive, photolabile oligodeoxyribonucleotide probe and its exploitation in identifying 50S ribosomal subunit components neighboring the alpha-sarcin loop. The probe is complementary to 23S rRNA nt 2653-2674. Photolysis of the complex formed between the probe and 50S subunits leads to site-specific probe photoincorporation into proteins L2, the most highly labeled protein, L1, L15, L16 and L27, labeled to intermediate extents, and L5, L9, L17 and L24, each labeled to a minor extent. Portions of each of these proteins thus lie within 23 A of nt U2653. These results lead us to conclude that the alpha-sarcin loop is located at the base of the L1 projection within the 50S subunit. Such placement, near the peptidyl transferase center, provides a rationale for the extreme sensitivity of ribosomal function to cleavage of the alpha-sarcin loop.

Topics: Affinity Labels; Azides; Binding Sites; DNA, Complementary; Endoribonucleases; Fungal Proteins; Genetic Complementation Test; Isotope Labeling; Nucleic Acid Conformation; Oligonucleotide Probes; Phosphorus Radioisotopes; RNA, Ribosomal; RNA, Ribosomal, 23S

1997

RNA present in post-ribosomal supernatants makes ribosomes susceptible to inactivation by gelonin and alpha-sarcin.

Biochemistry and molecular biology international, 1994, Volume: 32, Issue:3

The remarkable resistance of isolated ribosomes to gelonin is overcome by cofactors present in post-ribosomal supernatants. In rat liver post-ribosomal supernatant RNA is the cofactor responsible of the sensitization of ribosomes. Isolated RNA, which consists mostly of deacylated tRNA, accounts for less than 10 per cent of the activity of the original supernatant. The activity of the supernatant is completely destroyed by micrococcal nuclease and RNAase A and also by proteinase K, suggesting that some protein enhances the effect of RNA. RNA has a role also in the sensitization of ribosomes to alpha-sarcin, an RNAase which inactivates ribosomes by hydrolyzing a single phosphodiester bond in the same region of 28S rRNA which is the target of the N-glycosidase activity of gelonin.

Topics: Animals; Artemia; Autoradiography; Cytosol; Electrophoresis, Polyacrylamide Gel; Endopeptidase K; Endoribonucleases; Fungal Proteins; Liver; Molecular Weight; Phosphorus Radioisotopes; Plant Proteins; Protein Synthesis Inhibitors; Rabbits; Rats; Reticulocytes; Ribonuclease, Pancreatic; Ribosome Inactivating Proteins, Type 1; Ribosomes; RNA; RNA, Ribosomal; RNA, Ribosomal, 28S; RNA, Transfer; Serine Endopeptidases

1994