Modes of action of erythromycin and thiostrepton as inhibitors of protein synthesis

Cannon, Michael; Burns, Kay

doi:10.1016/0014-5793(71)80392-7

Cited by 25 publications

(5 citation statements)

References 16 publications

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“…However, in intact bacterial protoplasts, thiostrepton specifically inhibits the binding of aminoacyf-tRNA to ribosomes (5) and does not affect the translocation reaction even though this latter process involves, in part, the EF G-dependent guanosine triphosphatase (GTPase) reaction. Subsequently, similar selectivity was reported when thiostrepton (3) or siomycin (4) was added to a cell-free system actively synthesizing protein.…”

supporting

confidence: 60%

Inhibition of Ribosomal A Site Functions by Sporangiomycin and Micrococcin

Cundliffe

Dixon

1975

Antimicrob Agents Chemother

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Sporangiomycin and micrococcin inhibit the binding of aminoacyl-transfer ribonucleic acid into the ribosomal A site in intact bacterial protoplasts. They also prevent the assembly of [ribosome-elongation factor G-guanine nucleotide] complexes in vitro and compete with [(35)S]thiostrepton for ribosomal binding sites. We conclude that micrococcin and sporangiomycin block the ribosomal A site in the vicinity of the complex guanosine triphosphatase center and so resemble thiostrepton in their modes of action.

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supporting

confidence: 60%

Inhibition of Ribosomal A Site Functions by Sporangiomycin and Micrococcin

Cundliffe

Dixon

1975

Antimicrob Agents Chemother

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“…Difference in Interaction of Erythromycin with Free Ribosomes and with Polysomal Ribosomes. Earlier studies have already suggested that Ery fails to inhibit elongating ribosomes, for it had only a slight effect on amino acid incorporation by S30 extracts of Staphylococcus aureus (Mao and Putterman, 1968), Bacillus subtilis (Oleinick and Corcoran, 1970), or Escherichia coli (Cannon and Burns, 1971). However, the fragmented polysomes in such preparations have low overall endogenous activity, and so a significant fraction of the incorporation might reflect processes other than protein synthesis.…”

Section: Discussionmentioning

confidence: 99%

Selective action of erythromycin on initiating ribosomes

Tai¹,

Wallace²,

Davis³

1974

Biochemistry

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“…Thiostrepton inhibits protein translation by firmly binding to the complex formed by 23S rRNA and ribosomal protein L11 in bacterial ribosomes (Cannon and Burns, 1971; Cundliffe, 1971). The tsr gene encodes an RNA methyltransferase that prevents TSR from binding to ribosomes by 23S rRNA methylation (Thompson et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

A Cassette Containing Thiostrepton, Gentamicin Resistance Genes, and dif sequences Is Effective in Construction of Recombinant Mycobacteria

et al. 2017

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The genetic manipulation of Mycobacterium tuberculosis genome is limited by the availability of selection markers. Spontaneous resistance mutation rate of M. tuberculosis to the widely used kanamycin is relatively high which often leads to some false positive transformants. Due to the few available markers, we have created a cassette containing thiostrepton resistance gene (tsr) for selection in M. tuberculosis and M. bovis BCG, and gentamicin resistance gene (aacC1) for Escherichia coli and M. smegmatis mc2155, flanked with dif sequences recognized by the Xer system of mycobacteria. This cassette adds to the limited available selection markers for mycobacteria.

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Modes of action of erythromycin and thiostrepton as inhibitors of protein synthesis

Cited by 25 publications

References 16 publications

Inhibition of Ribosomal A Site Functions by Sporangiomycin and Micrococcin

Inhibition of Ribosomal A Site Functions by Sporangiomycin and Micrococcin

Selective action of erythromycin on initiating ribosomes

A Cassette Containing Thiostrepton, Gentamicin Resistance Genes, and dif sequences Is Effective in Construction of Recombinant Mycobacteria

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