Biosynthesis of 50 s ribosomal subunit in Escherichia coli

Osawa, Syozo; Otaka, Eiko; Itoh, Takuzì; Fukui, Takeshi

doi:10.1016/0022-2836(69)90158-2

Cited by 71 publications

(35 citation statements)

References 21 publications

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“…Chloramphenicol is the only other well studied antibiotic which affects ribosomal subunit assembly (18). In contrast with our findings, however, growth inhibition by chloramphenicol results in the incomplete assembly of both ribosomal subunits, consistent with a generalized effect on the translation of mRNAs for all ribosomal proteins (9).…”

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confidence: 55%

Macrolide antibiotics inhibit 50S ribosomal subunit assembly in Bacillus subtilis and Staphylococcus aureus

Champney

Burdine

1995

Antimicrob Agents Chemother

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Macrolide antibiotics are clinically important antibiotics which are effective inhibitors of protein biosynthesis in bacterial cells. We have recently shown that some of these compounds also inhibit 50S ribosomal subunit formation in Escherichia coli. Now we show that certain macrolides have the same effect in two gram-positive organisms, Bacillus subtilis and Staphylococcus aureus. Assembly in B. subtilis was prevented by erythromycin, clarithromycin, and azithromycin but not by oleandomycin. 50S subunit formation in S. aureus was prevented by each of seven structurally related 14-membered macrolides but not by lincomycin or two streptogramin antibiotics. Erythromycin treatment did not stimulate the breakdown of preformed 50S subunits in either organism. The formation of the 30S ribosomal subunit was also unaffected by these compounds. Assembly was also inhibited in a B. subtilis strain carrying a plasmid with the ermC gene that confers macrolide resistance by rRNA methylation. These results suggest that ribosomes contain an additional site for the inhibitory functions of macrolide antibiotics.

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contrasting

confidence: 55%

Macrolide antibiotics inhibit 50S ribosomal subunit assembly in Bacillus subtilis and Staphylococcus aureus

Champney

Burdine

1995

Antimicrob Agents Chemother

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“…It is known since a long time that application of translation inhibitors such as chloramphenicol (40,41) and erythromycin (42,43) provoke assembly defects of the large ribosomal subunit in E. coli . Albeit, it has been shown only recently that the two antibiotics cause assembly defects of both ribosomal subunits (14,44).…”

Section: Resultsmentioning

confidence: 99%

Validation of a fluorescence-based screening concept to identify ribosome assembly defects inEscherichia coli

et al. 2014

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While the structure of mature ribosomes is analyzed in atomic detail considerably less is known about their assembly process in living cells. This is mainly due to technical and conceptual hurdles. To analyze ribosome assembly in vivo, we designed and engineered an Escherichiacoli strain—using chromosomal gene knock-in techniques—that harbors large and small ribosomal subunits labeled with the fluorescent proteins EGFP and mCherry, respectively. A thorough characterization of this reporter strain revealed that its growth properties and translation apparatus were wild-type like. Alterations in the ratio of EGFP over mCherry fluorescence are supposed to indicate ribosome assembly defects. To provide proof of principle, subunit specific assembly defects were provoked and could be identified by both manual and fully automated fluorometric in vivo assays. This is to our knowledge the first methodology that directly detects ribosome assembly defects in vivo in a high-throughput compatible format. Screening of knock-out collections and small molecule libraries will allow identification of new ribosome assembly factors and possible inhibitors.

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“…Centrifugal fractionation of extracts from the cells as starvation proceeds reveals the steady accumulation of abnormal ribonucleoprotein particles, 'relaxed particles ', sedimenting between I 4 and 30 S (Dagley, Turnock & Wild, 1963). During methionine starvation, all the normal cellular RNA species continue to be synthesized and since few new mature ribosomes are formed the primary reason for the steady increase in the cellular RNA content is the accumulation of p16S and p23S rRNA (Adesnik & Levinthal, 1969;Chang & Irr, 1973;Dean & Sykes, 1974) which may be sub-methylated (Osawa et al, 1969). These precursor RNA forms are relatively …”

Section: Introductionmentioning

confidence: 99%

The Nature of the Proteins Present in the 'Relaxed Particles' from Methionine-starved Escherichia coli A19 (Hfr rel met rns)

Sykes

Metcalf

Pickering

1977

Journal of General Microbiology

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The ' relaxed particles ' formed during methionine starvation of Escherichia coli A I~ (Hfr re1 met rns) have been isolated by large-scale rate-zonal density gradient ultracentrifugation. The proteins and rRNA species associated with these particles have been examined.The rRNA species present are precursor and mature forms of I 6 S and 23 S rRNA. The bulk of the rRNA which accumulates during starvation is found within the particles. The proteins prepared directly from the particles give strong multiple immunoprecipitates with antisera specific to 30 S and 50 S ribosomal proteins. The soluble proteins, prepared and examined in the same manner, do not give this immunological reaction. Two-dimensional electrophoresis patterns of the proteins from the particles show that the proteins co-migrate with proteins from 30s and 50s ribosomes and are entirely dissimilar to the proteins prepared by the same methods from the soluble fraction of the cells. On the basis of these and other observations, it is concluded that the 'relaxed particles' are not artefacts but are arrested ribosome precursors containing both rRNA and certain ribosomal proteins.The free pool of ribosomal proteins is low in exponential-phase cells and is not significantly increased by a 2 h period of starvation for glucose.The implications of these observations concerning the proteins associated with 'relaxed' and 'chloramphenicol particles' are discussed in relation to ribosome biogenesis and the stabilization of rRNA.

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Biosynthesis of 50 s ribosomal subunit in Escherichia coli

Cited by 71 publications

References 21 publications

Macrolide antibiotics inhibit 50S ribosomal subunit assembly in Bacillus subtilis and Staphylococcus aureus

Macrolide antibiotics inhibit 50S ribosomal subunit assembly in Bacillus subtilis and Staphylococcus aureus

Validation of a fluorescence-based screening concept to identify ribosome assembly defects inEscherichia coli

The Nature of the Proteins Present in the 'Relaxed Particles' from Methionine-starved Escherichia coli A19 (Hfr rel met rns)

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