Suppression of polarity of insertion mutations within the gal operon of E. coli View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1977-01

AUTHORS

Jürgen Besemer, Maria Herpers

ABSTRACT

Phenotypic revertants of galOP::IS1 and galOP::IS2 mutations have been isolated after mutagenesis with nitrosoguanidine, they are probably caused by mutations in gene suA. The polarity suppressor mutations described in this study and a known mutation in gene suA isolated by D. Morse (Morse and Guertin, 1972) suppress polarity caused by IS1 more effectively than that caused by IS2 or IS4. Furthermore, suppressibility is influenced by the site and orientation of IS integration. The synthesis of the three enzymes in galOP::IS suA double mutants is constitutive and the ratio of the three enzymes is altered in comparison to the wild type. The reasons for constitutive synthesis of the galactose enzymes and for the altered ratio of enzyme synthesis are discussed. More... »

PAGES

295-304

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00268793

DOI

http://dx.doi.org/10.1007/bf00268793

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031434272

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/325374


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51 schema:description Phenotypic revertants of galOP::IS1 and galOP::IS2 mutations have been isolated after mutagenesis with nitrosoguanidine, they are probably caused by mutations in gene suA. The polarity suppressor mutations described in this study and a known mutation in gene suA isolated by D. Morse (Morse and Guertin, 1972) suppress polarity caused by IS1 more effectively than that caused by IS2 or IS4. Furthermore, suppressibility is influenced by the site and orientation of IS integration. The synthesis of the three enzymes in galOP::IS suA double mutants is constitutive and the ratio of the three enzymes is altered in comparison to the wild type. The reasons for constitutive synthesis of the galactose enzymes and for the altered ratio of enzyme synthesis are discussed.
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