Binding of dihydrostreptomycin to ribosomes and ribosomal subunits from streptomycin‐resistant mutants of <i>Chlamydomonas reinhardi</i>

Boschetti, Arminio; Bogdanov, Stefan

doi:10.1016/0014-5793(73)80502-2

Cited by 15 publications

(3 citation statements)

References 11 publications

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“…Although most antibiotics target organellar ribosomes, some of them affect cytoplasmic ribosomes. Cytosolic ribosomes bind to streptomycin, and form dimers and oligomers in Chlamydomonas reinhardtii (Boschetti and Bogdanov, 1973), and cytoplasmic protein synthesis in the lower eukaryote Tetrahymena thermophila is inhibited by paromomycin, an aminoglycoside antibiotic (Eustice and Wilhelm, 1984). These results suggest that cytosolic ribosomes are not resistant to these antibiotics, but are less sensitive to them.…”

Section: Discussionmentioning

confidence: 99%

APUM23, a nucleolar Puf domain protein, is involved in pre-ribosomal RNA processing and normal growth patterning in Arabidopsis

Abbasi¹,

Kim²,

Park³

et al. 2010

The Plant Journal

149

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SUMMARYPumilio, an RNA-binding protein that contains tandemly repeated Puf domains, is known to repress translational activity in early embryogenesis and polarized cells of non-plant species. Although Pumilio proteins have been characterized in many eukaryotes, their role in plants is unknown. In the present study, we characterized an Arabidopsis Pumilio-encoding gene, APUM23. APUM23 is constitutively expressed, with higher levels in metabolically active tissues, and its expression is up-regulated in the presence of either glucose or sucrose. The T-DNA insertion mutants apum23-1 and apum23-2 showed slow growth, with serrated and scrunched leaves, an abnormal venation pattern, and distorted organization of the palisade parenchyma cellsa phenotype that is reminiscent of nucleolin and ribosomal protein gene mutants. Intracellular localization studies indicate that APUM23 predominantly localizes to the nucleolus. Based on this localization, rRNA processing was examined. In apum23, 35S pre-rRNA, and unprocessed 18S and 5.8S poly(A) rRNAs, accumulated without affecting the steady-state levels of mature rRNAs, indicating that APUM23 is involved in the processing and/or degradation of 35S pre-rRNA and rRNA maturation by-products. The apum23 mutant showed increased levels of 18S rRNA biogenesis-related U3 and U14 small nucleolar RNAs (snoRNAs) and accumulated RNAs within the nucleolus. Our data suggest that APUM23 plays an important role in plant development via rRNA processing.

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Section: Discussionmentioning

confidence: 99%

APUM23, a nucleolar Puf domain protein, is involved in pre-ribosomal RNA processing and normal growth patterning in Arabidopsis

Abbasi¹,

Kim²,

Park³

et al. 2010

The Plant Journal

149

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show abstract

“…The antibiotic streptomycin interacts in Chlamydomonas reinhardii with chloroplastic and mitochondrial ribosomes; it may therefore be concluded that streptomycin resistance is caused by an alteration of these ribosomes (BOSCHETTI and BOGDANOV 1973b, BOSCHETTI et al 1973, SCHLANGER and SAGER 1974. This is confirmed by investigations of BOYNTON et al (1970), GiLLHAM et al (1970) and BOSCHETTI and BOGDANOV (1973 a, b), which show altered S-values of the chloroplastic ribosomes in mendelian and nonmendelian mutants.…”

Section: Discussionmentioning

confidence: 89%

Ribosomal proteins from the chloroplast of Chlamydomonas reinhardii and two streptomycin‐resistant mutants

Spiess

Arnold

1975

Berichte der Deutschen Botanischen Gesellschaft

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“…Although in E. coli a single ribosomal protein determines sensitivity to the antibiotic, the proper spatial organization of the SM binding site requires the interaction of a number of ribosomal proteins (9,39). Erythromycin (31) and SM (6) resistance in Chlamydomonas can apparently be determined by the alteration of one of a number of chloroplast ribosomal proteins, some of which appear to be coded in the chloroplast DNA (6,31,36). Given all of these facts, it is most likely that SMr results from a genetic change in the chloroplast DNA.…”

mentioning

confidence: 99%

Chloroplast and Cytoplasmic Ribosomes of Euglena : Selective Binding of Dihydrostreptomycin to Chloroplast Ribosomes

Schwartzbach

Schiff

1974

J Bacteriol

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Dihydrostreptomycin binds preferentially to chloroplast ribosomes of wild-type Euglena gracilis Klebs var. bacillaris Pringsheim. The K diss for the wild-type chloroplast ribosome-dihydrostreptomycin complex is 2 × 10 −7 M, a value comparable with that found for the Escherichia coli ribosome-dihydrostreptomycin complex. Chloroplast ribosomes isolated from the streptomycin-resistant mutant Sm 1 r BNgL and cytoplasmic ribosomes from wild-type have a much lower affinity for the antibiotic. The K diss for the chloroplast ribosome-dihydrostreptomycin complex of Sm 1 r is 387 × 10 −7 M, and the value for the cytoplasmic ribosome-dihydrostreptomycin complex of the wild type is 1,400 × 10 −7 M. Streptomycin competes with dihydrostreptomycin for the chloroplast ribosome binding site, and preincubation of streptomycin with hydroxylamine prevents the binding of streptomycin to the chloroplast ribosome. These results indicate that the inhibition of chloroplast development and replication in Euglena by streptomycin and dihydrostreptomycin is related to the specific inhibition of protein synthesis on the chloroplast ribosomes of Euglena .

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Binding of dihydrostreptomycin to ribosomes and ribosomal subunits from streptomycin‐resistant mutants of Chlamydomonas reinhardi

Cited by 15 publications

References 11 publications

APUM23, a nucleolar Puf domain protein, is involved in pre-ribosomal RNA processing and normal growth patterning in Arabidopsis

APUM23, a nucleolar Puf domain protein, is involved in pre-ribosomal RNA processing and normal growth patterning in Arabidopsis

Ribosomal proteins from the chloroplast of Chlamydomonas reinhardii and two streptomycin‐resistant mutants

Chloroplast and Cytoplasmic Ribosomes of Euglena : Selective Binding of Dihydrostreptomycin to Chloroplast Ribosomes

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