[Synthesis of specific proteins by the nucleoid of Escherichia coli].
The induction of beta-galactosidase and alkaline phosphatase by the nucleoid of Escherichia coli was studied. Only the membrane-associated form was active in the presence of S 30. The induction of beta-galactosidase showed an absolute requirement for the inducer and was enhanced by cyclic AMP and cyclic GMP. Further-more, in our hands, the synthetic activity of the membrane-associated nucleoid proved to be far higher than that of the soluble system described by Zubay. Our results suggest that membrane shield the structure which is necessary for the integrity of the initiation step of both transcription and translation.
D000469:Alkaline Phosphatase / Q000096:biosynthesis; D001426:Bacterial Proteins / Q000096:biosynthesis*; D002462:Cell Membrane / Q000502:physiology; D004926:Escherichia coli / Q000378:metabolism*; D005696:Galactosidases / Q000096:biosynthesis; D011132:Polyribosomes / Q000502:physiology; D014176:Protein Biosynthesis; D013347:Subcellular Fractions / Q000378:metabolism; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D000469:Alkaline Phosphatase; D005696:Galactosidases
Synthèse de protéines spécifiques par le nucléoide d'Escherichia coli.