Evidence for a conformational change in the 30 S <i>E. coli</i> ribosomal subunit upon formation of 70 S particles

Litman, David J.; Lee, Chien C.; Cantor, Charles R.

doi:10.1016/0014-5793(74)81027-6

Cited by 34 publications

(11 citation statements)

References 15 publications

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“…In spite of this difference, the distribution of 125 1 among the ribosomal proteins (table 1) was reproducible in 7 different experiments performed with 2 independent preparations of ribosomes. However, it differs from iodination patterns reported [9,10,16], probably due to our different experimental conditions. Streptomycin and viomycin did not appreciably affect the total incorporation of 125 I by 70 S ribosomes (not shown).…”

Section: Resultscontrasting

confidence: 92%

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Streptomycin‐ and viomycin‐induced conformational changes of ribosomes detected by iodination

1978

FEBS Letters

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Section: Resultscontrasting

confidence: 92%

“…The validity of this method for the study of structural modifications of the ribosome has already been established [9,10]. We have found that the binding of either streptomycin or viomycin to 70 S ribosomes from Escherichia coli modifies the iodination of at least 5 or 9 ribosomal proteins, respectively.…”

Section: Introductionmentioning

confidence: 94%

Streptomycin‐ and viomycin‐induced conformational changes of ribosomes detected by iodination

1978

FEBS Letters

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“…It has been reported that upon formation of the 70S ribosome a conformational change of the subparticles can take place (see, e.g. Michalski and Sells, 1975 ;Litman et al, 1974;Chang, 1973 ;etc.). However, in our opinion it seems unlikely that this conformational change could significantly influence the effectivity of subparticle labelling because we used a chemically non-specific reagent.…”

Section: H Specificity Of the Sin-analog Photoreaction With Ribosomamentioning

confidence: 99%

Identification of components of the streptomycin-binding center ofE. coli MRE 600 ribosomes by photo-affinity labelling

Girshovich¹,

Bochkareva²,

Ovchinnikov³

1976

Molec. Gen. Genet.

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The [H3]-labelled photo-activated analog of streptomycin (photo-Sm) is obtained as a result of the streptomycin reaction with 2-nitro, 4-azidobenzoylhydrazide and subsequent reduction with NaBH34. The analog retains the functional activity of the initial antibiotic as judged by two criteria: (1) it binds only to the 30S subparticle of ribosomes and (2) it inhibits the factor-free ("non-enzymatic") PCMB-stimulated polyU-dependent system of translation (Gavrilova and Spirin, 1971). After irradiation of the reaction mixture containing photo-Sm and either the 30S or 50S subparticles of ribosomes under similar conditions, the analog covalently binds chiefly to the 30S subparticle. Irradiation of the photo-Sm mixture with whole 70S ribosomes leads to a uniform distribution of a covalently bound label among the subparticles. A comparison of the effects obtained allows the conclusion that the analog is located on the interface of the ribosomal subparticles. In the 30S subparticle the photo-Sm attacks mainly the protein component (more than 95% of all the covalently bound label). The proteins labelled by photo-reaction are identified as S7 (main), S14 (additional) and S16/S17 (minor).

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“…The preparation and characterization of the fluorescein isothiocyanate derivative of erythromycyl amine (F-ery) have been described previously (14,15). Ribosomes were prepared from E. coli MRE600 as tight couples (17) or salt washed (18).…”

Section: Introductionmentioning

confidence: 99%

Ribosome binding by tRNAs with fluorescent labeled 3′ termini

Wells

Cantor

1980

Nucl Acids Res

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Yeast and E. coli tRNAPhe samples were oxidized and labeled at the 3' end with dansyl hydrazine or fluorescein thiosemicarbazide. These tRNAs can bind to poly(U)-programmed E. coli 70S tight couple ribosomes in 25 mM magnesium at 8 degrees C. Two binding sites with binding constants of about 1 X 10(9) M-1 (P) and 3 X 10(7) M-1 (A) were determined for the yeast tRNAPhe derivatives. With E. coli tRNAPhe the A site affinity is similar to yeast tRNAPhe but the P site affinity is 5-fold weaker. Singlet-singlet energy transfer showd that the distance from the 3' end of tRNAPhe in the P site to a fluorescein derivative of erythromycin is 23 A. This supports in vitro studies suggesting that erythromycin binds near the peptide moiety of peptidyl tRNA. A distance of 34 A between the 3' ends of 2 tRNAs bound simulatneously on the ribosome was also measured. This long distance may mean that the deacylated fluorescent tRNA binds to the A site in an orientation like that in the stringent response rather than in protein synthesis.

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Evidence for a conformational change in the 30 S E. coli ribosomal subunit upon formation of 70 S particles

Cited by 34 publications

References 15 publications

Streptomycin‐ and viomycin‐induced conformational changes of ribosomes detected by iodination

Streptomycin‐ and viomycin‐induced conformational changes of ribosomes detected by iodination

Identification of components of the streptomycin-binding center ofE. coli MRE 600 ribosomes by photo-affinity labelling

Ribosome binding by tRNAs with fluorescent labeled 3′ termini

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