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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1966-2-19
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pubmed:abstractText |
Curtiss, Roy, III (Oak Ridge National Laboratory, Oak Ridge, Tenn.), Leigh J. Charamella, Claire M. Berg, and Paula E. Harris. Kinetic and genetic analyses of d-cycloserine inhibition and resistance in Escherichia coli. J. Bacteriol. 90:1238-1250.1965.-Wild-type cells of Escherichia coli growing at 37 C in mineral salts-glucose medium with vigorous aeration were lysed at maximal exponential rates by 10(-4) to 10(-2)md-cycloserine. At concentrations above 2 x 10(-2)m, d-cycloserine was bacteriostatic. Low levels of d-cycloserine (10(-5)m) and pencillin G (10 units per ml) interacted synergistically to cause a rapid exponential rate of lysis. Spontaneous mutations to d-cycloserine resistance occurred in discrete steps at frequencies of 10(-6) to 10(-7) for each step. First-, second-, and third-step d-cycloserine-resistant mutants were lysed at maximal exponential rates by d-cycloserine concentrations of 10(-3), 3 x 10(-3), and 5 x 10(-3)m, respectively. d-Alanine, l-alanine, and dl-alanyl-dl-alanine reversed d-cycloserine-induced lysis, in that order of effectiveness. On the basis of these observations, a d-cycloserine-enrichment cycling technique was developed for isolation of auxotrophic mutants. d-Cycloserine at 2 x 10(-3)m was as efficient as penicillin G (1,000 units per ml) for mutant enrichment in E. coli and should be useful for isolation of mutants in penicillin-resistant microorganisms. Bacterial conjugation experiments indicated that all three mutations conferring d-cycloserine resistance were linked to the met(1) locus. Transduction experiments showed that the mutation conferring first-step resistance was at least 0.5 min away from the mutations conferring second- and third-step resistance. The latter two mutations possibly occurred in the same gene, since they were sometimes carried in the same transducing phage. Studies on expression of d-cycloserine resistance indicated that these mutations were neither dominant nor recessive to each other nor to the d-cycloserine-sensitivity allele. Each allelic state exerted its influence on the phenotype independently of the others. These results are discussed in terms of the known inhibition of alanine racemase and d-alanyl-d-alanine synthetase by d-cycloserine.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-13267987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-13485077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-13795638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-13796629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-13851300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-13872629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14042952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14047211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14221875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14255660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14255678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14362438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14446135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14467046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14479178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-14927572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-15436457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-16561951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-16562043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5321479-17247995
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9193
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1238-50
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:5321479-Alanine,
pubmed-meshheading:5321479-Coliphages,
pubmed-meshheading:5321479-Cycloserine,
pubmed-meshheading:5321479-Escherichia coli,
pubmed-meshheading:5321479-Kinetics,
pubmed-meshheading:5321479-Mutation,
pubmed-meshheading:5321479-Penicillin Resistance,
pubmed-meshheading:5321479-Penicillins
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pubmed:year |
1965
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pubmed:articleTitle |
Kinetic and genetic analyses of D-cycloserine inhibition and resistance in Escherichia coli.
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pubmed:publicationType |
Journal Article,
In Vitro
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