Bibliothek

feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
Filter
  • Digitale Medien  (3)
  • 1975-1979  (3)
Materialart
  • Digitale Medien  (3)
Erscheinungszeitraum
Jahr
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 152 (1977), S. 205-210 
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary A λ phage has been isolated which specifically transduces the Escherichia coli pheS and pheT genes coding for the α and β subunits of the phenylalanyl-tRNA synthetase (PRS). This phage transduces with high frequency (i) several temperaturesensitive PRS mutants to thermoresistance and (ii) a p-fluorophenylalanine resistant PRS mutant to sensitivity against this amino-acid analog. The in vitro PRS activities of such lysogens suggest that the α and β subunits coded by the transducing phage complement the mutant host PRS-subunits in vivo by means of formation of hybrid enzymes. The transducing λ phages were also used to infect UV light irradiated cells. The SDS-gel electrophoretic analysis of the proteins synthesized in such cells revealed that the phage codes at least for four different E. coli proteins. Two proteins with molecular weights of 94,000 and 38,000 daltons cross-reacted with an anti PRS serum and were thus identified as the β and α subunits of PRS, respectively. A third protein with w molecular weight of 22,000 daltons is identical with the ribosomal initiation factor IF3 (Springer et al., 1977b). The other protein (Mr 78,000) is still unidentified.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 151 (1977), S. 17-26 
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary A thermosensitive E. coli mutant is described which has at least two defects in vitro: a thermolabile initiation factor IF3 activity and a modified L-phenylalanine: tRNAPhe ligase (EC 6.1.1.20) activity. These two defects cotransduce and are located near 38 min on the new E. coli map. Thermoresistant revertants showing in vitro reversion for one defect also revert in vitro for the other defect. The thermosensitive mutation is recessive to its wild type allele, and in vitro analysis of wild type/mutant heterodiploïds also show reversion for both defects.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 169 (1979), S. 337-343 
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary A set of λ transducing phages carrying varying lengths of the E. coli chromosome around the structural gene for initiation factor IF3 (infC) was derived from λp2 which is known to cary, besides infC, the structural genes for the α subunit of phenylalanyl-tRNA synthetase (pheS), the β subunit of phenylalanyl-tRNA synthetase (phetT) and the structural gene for threonyl-tRNA synthetase (thrS). The E. coli coding content of these derived phages was analysed by genetic complementation of a set of mutants and by SDS-polyacrylamide gel analysis of the proteins synthesized in UV irradiated cells infected with these phages. The segregation pattern of the different genes among these derived phages indicates that the order of the genes is pheT-pheS-“P12”-(infC, thrS) where infC is probably between “P12” and thrS. “P12” is the structural gene of a 12,000 molecular weight unidentified protein.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
    BibTip Andere fanden auch interessant ...
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...