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dc.contributor.authorJimenez, A.
dc.contributor.authorTipper, Donald J.
dc.contributor.authorDavies, J.
dc.date2022-08-11T08:09:18.000
dc.date.accessioned2022-08-23T16:26:06Z
dc.date.available2022-08-23T16:26:06Z
dc.date.issued1973-06-01
dc.date.submitted2019-06-27
dc.identifier.citation<p>Antimicrob Agents Chemother. 1973 Jun;3(6):729-38. doi: 10.1128/aac.3.6.729. <a href="https://doi.org/10.1128/aac.3.6.729">Link to article on publisher's site</a></p>
dc.identifier.issn0066-4804 (Linking)
dc.identifier.doi10.1128/aac.3.6.729
dc.identifier.pmid4597739
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36492
dc.description.abstractThe sulfur-containing antibiotic thiolutin has been shown to be a potent, reversible inhibitor of the growth of Saccharomyces cerevisiae. Viability was unaffected over the concentration range of 4 to 100 mug/ml. At concentrations as low as 2 mug/ml, the drug inhibited ribonucleic acid (RNA) and protein synthesis in whole cells and spheroplasts. At these low concentrations, protein synthesis continued for a short period of time after RNA synthesis was completely stopped. With higher drug concentrations (greater than 20 mug/ml) protein synthesis was inhibited; concentrations of thiolutin up to 100 mug/ml did not affect translocation or peptide bond formation in cell-free protein-synthesizing systems from yeast. The effect of thiolutin on the activity of partially purified deoxyribonucleic acid-dependent RNA polymerases was examined, and the drug was found to be a potent inhibitor of RNA synthesis in vitro. Inhibition was greatest when the polymerase was preincubated with thiolutin. Several mechanisms are discussed to explain the multiple effects of thiolutin on S. cerevisiae. Since the action of the drug is easily reversed, thiolutin may prove to be of use in studies of various stages of yeast growth.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=4597739&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 1973, American Society for Microbiology. Publisher PDF posted as allowed by the publisher's copyright policy at https://journals.asm.org/content/copyright-transfer-and-supplemental-material-license-agreement-2017.
dc.subjectMicrobiology
dc.subjectPhysiology
dc.titleMode of action of thiolutin, an inhibitor of macromolecular synthesis in Saccharomyces cerevisiae
dc.typeJournal Article
dc.source.journaltitleAntimicrobial agents and chemotherapy
dc.source.volume3
dc.source.issue6
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1054&amp;context=maps_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/54
dc.identifier.contextkey14823792
refterms.dateFOA2022-08-23T16:26:06Z
html.description.abstract<p>The sulfur-containing antibiotic thiolutin has been shown to be a potent, reversible inhibitor of the growth of Saccharomyces cerevisiae. Viability was unaffected over the concentration range of 4 to 100 mug/ml. At concentrations as low as 2 mug/ml, the drug inhibited ribonucleic acid (RNA) and protein synthesis in whole cells and spheroplasts. At these low concentrations, protein synthesis continued for a short period of time after RNA synthesis was completely stopped. With higher drug concentrations (greater than 20 mug/ml) protein synthesis was inhibited; concentrations of thiolutin up to 100 mug/ml did not affect translocation or peptide bond formation in cell-free protein-synthesizing systems from yeast. The effect of thiolutin on the activity of partially purified deoxyribonucleic acid-dependent RNA polymerases was examined, and the drug was found to be a potent inhibitor of RNA synthesis in vitro. Inhibition was greatest when the polymerase was preincubated with thiolutin. Several mechanisms are discussed to explain the multiple effects of thiolutin on S. cerevisiae. Since the action of the drug is easily reversed, thiolutin may prove to be of use in studies of various stages of yeast growth.</p>
dc.identifier.submissionpathmaps_pubs/54
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Microbiology
dc.source.pages729-38


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