• Medientyp: E-Artikel
  • Titel: Fatty Acid Degradation in Escherichia coli : Requirement of Cyclic Adenosine Monophosphate and Cyclic Adenosine Monophosphate Receptor Protein for Enzyme Synthesis
  • Beteiligte: Pauli, Georg; Ehring, Ruth; Overath, Peter
  • Erschienen: American Society for Microbiology, 1974
  • Erschienen in: Journal of Bacteriology
  • Sprache: Englisch
  • DOI: 10.1128/jb.117.3.1178-1183.1974
  • ISSN: 0021-9193; 1098-5530
  • Schlagwörter: Molecular Biology ; Microbiology
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: <jats:p> The strong repression of inducible synthesis of the enzymes of fatty acid degradation by glucose can be partially relieved by the addition of cyclic adenosine 3′,5′ monophosphate (cyclic AMP) to the growth medium. This reversal of the glucose effect by cyclic AMP is <jats:italic>not</jats:italic> observed in a mutant (K29) that is unable to grow on fatty acids as sole carbon source and that was found to synthesize low levels of several enzymes specified by the <jats:italic>fad</jats:italic> regulon. In a revertant selected for the ability to grow on oleate these effects are concomitantly relieved. By both genetic (co-transduction of the mutation with the <jats:italic>strA</jats:italic> locus) and biochemical experiments (an extract of the mutant strain does not show the cyclic AMP-dependent stimulation of the deoxyribonucleic acid-directed in vitro synthesis of the enzymes of the <jats:italic>gal</jats:italic> operon), it is demonstrated that the mutant lacks functional cyclic AMP receptor protein (CR protein). It is concluded that, like many other inducible enzyme systems, expression of the enzymes of the <jats:italic>fad</jats:italic> system requires cyclic AMP and the CR protein. </jats:p>
  • Zugangsstatus: Freier Zugang