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dc.contributor.authorTipper, Donald J.
dc.contributor.authorJohnson, C. W.
dc.contributor.authorGinther, C. L.
dc.contributor.authorLeighton, T.
dc.contributor.authorWittmann, H. G.
dc.date2022-08-11T08:09:18.000
dc.date.accessioned2022-08-23T16:26:09Z
dc.date.available2022-08-23T16:26:09Z
dc.date.issued1977-01-18
dc.date.submitted2019-06-27
dc.identifier.citation<p>Mol Gen Genet. 1977 Jan 18;150(2):147-59. DOI: 10.1007/BF00695395</p>
dc.identifier.issn0026-8925 (Linking)
dc.identifier.doi10.1007/BF00695395
dc.identifier.pmid402547
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36502
dc.description.abstractAll of several hundred erythromycin resistant single site mutants of Bacillus subtilis W168 are temperature senstive for sporulation. The mutants and wild type cells grow vegetatively at essentially the same rates at both permissive (30 degrees C) and nonpermissive (47 degrees C) temperatures. In addition cellular protein synthesis, cell mass increases and cell viabilities are similar in mutant and wild type strains for several hours after the end of vegetative growth (47 degrees C). in the mutants examined, the temperature sensitive periods begin when the sporulation process is approximately 40% completed, and end when the process is 90% completed. At nonpermissive temperatures, the mutants produce serine and metal proteases at 50% of the wild type rate, accumulate serine esterase at 16% of the wild type rate, and do not demonstrate a sporulation related increase in alkaline phosphatase activity. The eryR and spots phenotypes cotransform 100%, and cotransduce 100% using phage PBS1. Revertants selected for ability to sporulate normally at 47 degrees C (spot), simultaneously regain parental sensitivity to erthromycin. No second site revertants are found. Ribosomes from eryR spots strains bind erythromycin at less than 1% of the wild type rate. A single 50S protein (L17) from mutant ribosomes shows an altered electrophoretic mobility. Ribosomes from spo+ revertants bind erythromycin like parental ribosomes and their proteins are electrophoretically identical to wild type. These data indicate that the L17 protein of the 50S ribosomal subunit from Bacillus subtilis may participate specifically in the sporulation process.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=402547&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1007/BF00695395
dc.subjectGenetics and Genomics
dc.subjectMicrobiology
dc.subjectPhysiology
dc.titleErythromycin resistant mutations in Bacillus subtilis cause temperature sensitive sporulation
dc.typeJournal Article
dc.source.journaltitleMolecular and general genetics : MGG
dc.source.volume150
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/63
dc.identifier.contextkey14823818
html.description.abstract<p>All of several hundred erythromycin resistant single site mutants of Bacillus subtilis W168 are temperature senstive for sporulation. The mutants and wild type cells grow vegetatively at essentially the same rates at both permissive (30 degrees C) and nonpermissive (47 degrees C) temperatures. In addition cellular protein synthesis, cell mass increases and cell viabilities are similar in mutant and wild type strains for several hours after the end of vegetative growth (47 degrees C). in the mutants examined, the temperature sensitive periods begin when the sporulation process is approximately 40% completed, and end when the process is 90% completed. At nonpermissive temperatures, the mutants produce serine and metal proteases at 50% of the wild type rate, accumulate serine esterase at 16% of the wild type rate, and do not demonstrate a sporulation related increase in alkaline phosphatase activity. The eryR and spots phenotypes cotransform 100%, and cotransduce 100% using phage PBS1. Revertants selected for ability to sporulate normally at 47 degrees C (spot), simultaneously regain parental sensitivity to erthromycin. No second site revertants are found. Ribosomes from eryR spots strains bind erythromycin at less than 1% of the wild type rate. A single 50S protein (L17) from mutant ribosomes shows an altered electrophoretic mobility. Ribosomes from spo+ revertants bind erythromycin like parental ribosomes and their proteins are electrophoretically identical to wild type. These data indicate that the L17 protein of the 50S ribosomal subunit from Bacillus subtilis may participate specifically in the sporulation process.</p>
dc.identifier.submissionpathmaps_pubs/63
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Microbiology
dc.source.pages147-59


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