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  • Saccharomyces cerevisiae  (2)
  • DNA integration  (1)
  • Springer  (2)
  • American Institute of Physics
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Verlag/Herausgeber
  • Springer  (2)
  • American Institute of Physics
Erscheinungszeitraum
  • 1
    ISSN: 1432-0983
    Schlagwort(e): Trans-kingdom conjugation ; DNA integration ; Saccharomyces cerevisiae ; Escherichia coli
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary IncQ-derived conjugative shuttle vectors, which carried the yeast gene URA3 and/or the yeast autonomously replicating sequence (ARS1), were constructed. Both the ars-plus plasmid pAY205 and the ars-less plasmid pAY201 were successfully transmitted from E. coli to S. cerevisiae by the action of mob and tra. In this trans-kingdom conjugation, plasmid pAY205 could replicate and be retained in transconjugants. Plasmid pAY201 caused the formation of “micro-colonies” of abortive transconjugants due to its transient expression and rapid disappearance. Nevertheless, one per about 103 colonies caused by transmitted pAY201 plasmids were uncurable by integration into the homologous region of a yeast chromosome. Analyses by restriction enzyme mapping and Southern hybridization indicate that this integration is primarily caused by a double crossover during conjugation and not by a single reciprocal recombination.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    ISSN: 1432-072X
    Schlagwort(e): Agglutination substance ; Cell-cell recognition ; Glycoprotein ; Mating ; Saccharomyces cerevisiae ; Sexual agglutinability ; Yeast
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract An a-mating-type-specific substance responsible for sexual agglutination was purified to 397-times in specific activity (units/mg protein) from the cytoplasm of a-mating type cells. The purified substance gave a single band stained with PAS reagent but not with both Coomassie brilliant blue and silver staining reagent by polyacrylamide gel electrophoresis in the presence of 8 M urea. However, incorporation of [35S]methionine and Lowry reaction clearly indicate that the substance is a glycoprotein. The substance specifically masked sexual agglutinability of cells of the opposite mating type α, indicating univalent action. The substance is a glycoprotein with a carbohydrate content of 90%, a pI of 4.5, and a molecular weight of 130,000. The substance was inactivated by 2-mercaptoethanol and proteolytic enzymes but not by glycolytic enzymes. The substance formed a complementary complex having no biological activity when mixed with α-agglutination substance from the wall or cytoplasm of α-cells in vitro.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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