Kinetics of the onset of catabolite repression in Escherichia coli as determined by lac messenger ribonucleic acid initiations and intracellular cyclic adenosine 3',5'-monophosphate levels.

نویسندگان

  • D M Haggerty
  • R F Schleif
چکیده

The rates of synthesis of beta-galactosidase (EC 3.2.1.23) and the intracellular levels of cyclic 3',5'-adenosine monophosphate (cAMP) soon after the addition of glucose or glycerol to exponentially growing cultures of Escherichia coli have been determined. Within 10 s of its addition, glucose, but not glycerol, lowered the apparent initiation frequency of lac messenger ribonucleic acid. The glucose-generated reduction in initiations is identified as catabolite repression by its reversibility with cAMP. The intracellular cAMP levels respond virtually identically to glucose and glycerol additions. Thus, no correlation was observed between the rate of messenger ribonucleic acid initiation and the level of cAMP.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Accumulation of untranslated lactose-specific messenger ribonucleic acid during catabolite repression in Escherichia coli.

When Escherichia coli K-12 Hfr.H was induced to synthesize beta-galactosidase in the presence of glucose, an untranslated lactose-specific mRNA (lac-mRNA), protected from decay, was found to accumulate progressively within the cells. The lac-mRNA accumulation was unaffected by the carbon source on which the cells had been grown before the induction. The amount of the lac-mRNA available for tran...

متن کامل

Cyclic adenosine monophosphate-independent mutants of the lactose operon of Escherichia coli.

In Escherichia coli the transcription of the lactose operon, like other catabolite-sensitive operons, requires catabolite gene activator protein and 3',5'-cyclic adenosine monophosphate in addition to ribonucleic acid polymerase. We isolated and analyzed lac(+) revertants from a crp(-) strain of E. coli. We found that revertants with a higher level of expression only for the lac operon lie in t...

متن کامل

Regulation of P-Galactosidase Synthesis in Escherichia coli by Cyclic Adenosine 3’, 5’-Monophosphate

Cyclic adenosine 3’,5’-monophosphate (cyclic AMP) increases the differential rate of synthesis of @-galactosidase in Escherichia coli made permeable by treatment with t&(hydroxymethyl)aminomethane and ethylenediaminetetraacetic acid. In normal, growing cells, cyclic AMP overcomes the transient repression of /3-galactosidase by glucose. A half-maximal effect of cyclic AMP occurs at about 7 x 10-...

متن کامل

Regulation of beta-galactosidase synthesis in Escherichia coli by cyclic adenosine 3',5'-monophosphate.

Cyclic adenosine 3’,5’-monophosphate (cyclic AMP) increases the differential rate of synthesis of @-galactosidase in Escherichia coli made permeable by treatment with t&(hydroxymethyl)aminomethane and ethylenediaminetetraacetic acid. In normal, growing cells, cyclic AMP overcomes the transient repression of /3-galactosidase by glucose. A half-maximal effect of cyclic AMP occurs at about 7 x 10-...

متن کامل

Adenosine 3':5'-cyclic monophosphate as mediator of catabolite repression in Escherichia coli.

Measurements of intracellular adenosine 3':5'-cyclic monophosphate (cAMP) concentrations in E. coli under a variety of conditions show that levels of this nucleotide are well correlated with the rate of synthesis of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23) in both catabolite repression and transient repression. These results, combined with extensive genetic and in v...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Journal of bacteriology

دوره 123 3  شماره 

صفحات  -

تاریخ انتشار 1975