Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria
Zagórski, W. ; Boguta, M. ; Mieszczak, M. ; Claisse, M. ; Guiard, B. ; Spyridakis, A. ; Slonimski, P. P.
Springer
Published 1987
Springer
Published 1987
| ISSN: |
1432-0983
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|---|---|
| Keywords: |
Yeast ; Mitochondria ; Translation ; Informational Suppression
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| Source: |
Springer Online Journal Archives 1860-2000
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| Topics: |
Biology
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| Notes: |
Summary Phenotypic suppression by the antibiotic, paromomycin, of the mitochondrial oxi1 −-V25 mutation, a mutation which arrests by premature ochre codon the synthesis of the cox 11 subunit, was studied in isolated yeast mitochondria competent in translation. This antibiotic is known to suppress the mutation in vivo (Dujardin et al. 1984) and allowed in vitro, at concentrations of 20–1100 Mg per ml. the synthesis of the cox II subunit. This strongly suggests that phenotypic suppression of mit − mutations is due to the direct action of paromomycin on mitochondrial ribosomes. The effect of paromomycin bears a resemblance to the function of the omnipotent nuclear suppressor mutation R705. The nuclear suppression was expressed in isolated mitochondria; suppressor mutation influenced the structure of the mitoribosome. Therefore, it appears that mitoribosomes are indeed the common target in the phenotypical and genetic nuclear suppression of the oxi1-V25 mutation.
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798295557752487937 |
|---|---|
| autor | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. |
| autorsonst | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. |
| book_url | http://dx.doi.org/10.1007/BF00405752 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM203112962 |
| issn | 1432-0983 |
| journal_name | Current genetics |
| materialart | 1 |
| notes | Summary Phenotypic suppression by the antibiotic, paromomycin, of the mitochondrial oxi1 −-V25 mutation, a mutation which arrests by premature ochre codon the synthesis of the cox 11 subunit, was studied in isolated yeast mitochondria competent in translation. This antibiotic is known to suppress the mutation in vivo (Dujardin et al. 1984) and allowed in vitro, at concentrations of 20–1100 Mg per ml. the synthesis of the cox II subunit. This strongly suggests that phenotypic suppression of mit − mutations is due to the direct action of paromomycin on mitochondrial ribosomes. The effect of paromomycin bears a resemblance to the function of the omnipotent nuclear suppressor mutation R705. The nuclear suppression was expressed in isolated mitochondria; suppressor mutation influenced the structure of the mitoribosome. Therefore, it appears that mitoribosomes are indeed the common target in the phenotypical and genetic nuclear suppression of the oxi1-V25 mutation. |
| package_name | Springer |
| publikationsjahr_anzeige | 1987 |
| publikationsjahr_facette | 1987 |
| publikationsjahr_intervall | 8014:1985-1989 |
| publikationsjahr_sort | 1987 |
| publisher | Springer |
| reference | 12 (1987), S. 305-310 |
| schlagwort | Yeast Mitochondria Translation Informational Suppression |
| search_space | articles |
| shingle_author_1 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. |
| shingle_author_2 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. |
| shingle_author_3 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. |
| shingle_author_4 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. |
| shingle_catch_all_1 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria Yeast Mitochondria Translation Informational Suppression Yeast Mitochondria Translation Informational Suppression Summary Phenotypic suppression by the antibiotic, paromomycin, of the mitochondrial oxi1 −-V25 mutation, a mutation which arrests by premature ochre codon the synthesis of the cox 11 subunit, was studied in isolated yeast mitochondria competent in translation. This antibiotic is known to suppress the mutation in vivo (Dujardin et al. 1984) and allowed in vitro, at concentrations of 20–1100 Mg per ml. the synthesis of the cox II subunit. This strongly suggests that phenotypic suppression of mit − mutations is due to the direct action of paromomycin on mitochondrial ribosomes. The effect of paromomycin bears a resemblance to the function of the omnipotent nuclear suppressor mutation R705. The nuclear suppression was expressed in isolated mitochondria; suppressor mutation influenced the structure of the mitoribosome. Therefore, it appears that mitoribosomes are indeed the common target in the phenotypical and genetic nuclear suppression of the oxi1-V25 mutation. 1432-0983 14320983 Springer |
| shingle_catch_all_2 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria Yeast Mitochondria Translation Informational Suppression Yeast Mitochondria Translation Informational Suppression Summary Phenotypic suppression by the antibiotic, paromomycin, of the mitochondrial oxi1 −-V25 mutation, a mutation which arrests by premature ochre codon the synthesis of the cox 11 subunit, was studied in isolated yeast mitochondria competent in translation. This antibiotic is known to suppress the mutation in vivo (Dujardin et al. 1984) and allowed in vitro, at concentrations of 20–1100 Mg per ml. the synthesis of the cox II subunit. This strongly suggests that phenotypic suppression of mit − mutations is due to the direct action of paromomycin on mitochondrial ribosomes. The effect of paromomycin bears a resemblance to the function of the omnipotent nuclear suppressor mutation R705. The nuclear suppression was expressed in isolated mitochondria; suppressor mutation influenced the structure of the mitoribosome. Therefore, it appears that mitoribosomes are indeed the common target in the phenotypical and genetic nuclear suppression of the oxi1-V25 mutation. 1432-0983 14320983 Springer |
| shingle_catch_all_3 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria Yeast Mitochondria Translation Informational Suppression Yeast Mitochondria Translation Informational Suppression Summary Phenotypic suppression by the antibiotic, paromomycin, of the mitochondrial oxi1 −-V25 mutation, a mutation which arrests by premature ochre codon the synthesis of the cox 11 subunit, was studied in isolated yeast mitochondria competent in translation. This antibiotic is known to suppress the mutation in vivo (Dujardin et al. 1984) and allowed in vitro, at concentrations of 20–1100 Mg per ml. the synthesis of the cox II subunit. This strongly suggests that phenotypic suppression of mit − mutations is due to the direct action of paromomycin on mitochondrial ribosomes. The effect of paromomycin bears a resemblance to the function of the omnipotent nuclear suppressor mutation R705. The nuclear suppression was expressed in isolated mitochondria; suppressor mutation influenced the structure of the mitoribosome. Therefore, it appears that mitoribosomes are indeed the common target in the phenotypical and genetic nuclear suppression of the oxi1-V25 mutation. 1432-0983 14320983 Springer |
| shingle_catch_all_4 | Zagórski, W. Boguta, M. Mieszczak, M. Claisse, M. Guiard, B. Spyridakis, A. Slonimski, P. P. Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria Yeast Mitochondria Translation Informational Suppression Yeast Mitochondria Translation Informational Suppression Summary Phenotypic suppression by the antibiotic, paromomycin, of the mitochondrial oxi1 −-V25 mutation, a mutation which arrests by premature ochre codon the synthesis of the cox 11 subunit, was studied in isolated yeast mitochondria competent in translation. This antibiotic is known to suppress the mutation in vivo (Dujardin et al. 1984) and allowed in vitro, at concentrations of 20–1100 Mg per ml. the synthesis of the cox II subunit. This strongly suggests that phenotypic suppression of mit − mutations is due to the direct action of paromomycin on mitochondrial ribosomes. The effect of paromomycin bears a resemblance to the function of the omnipotent nuclear suppressor mutation R705. The nuclear suppression was expressed in isolated mitochondria; suppressor mutation influenced the structure of the mitoribosome. Therefore, it appears that mitoribosomes are indeed the common target in the phenotypical and genetic nuclear suppression of the oxi1-V25 mutation. 1432-0983 14320983 Springer |
| shingle_title_1 | Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria |
| shingle_title_2 | Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria |
| shingle_title_3 | Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria |
| shingle_title_4 | Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T09:38:06.530Z |
| titel | Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria |
| titel_suche | Phenotypic suppression and nuclear accommodation of the mit − oxi1-V25 mutation in isolated yeast mitochondria |
| topic | W |
| uid | nat_lic_papers_NLM203112962 |