Current Microbiology

, Volume 21, Issue 2, pp 131–137 | Cite as

Genetic regulation of glycogen biosynthesis inEscherichia coli: In vivo effects of the catabolite repression and stringent response systems inglg gene expression

  • Tony Romeo
  • Jill Black
  • Jack Preiss


The synthesis of two of theEscherichia coli glycogen biosynthetic enzymes, ADPglucose pyrophosphorylase (glgC) and glycogen synthase (glgA) was activated by the addition of 5 mM cyclic AMP (cAMP) to maxicells; synthesis of glycogen branching enzyme (glgB) was unaffected.β-Galactosidase activity expressed from a gene fusion,φ(glgC-lacZ), was approximately five-fold higher in acya+ versus an isogeniccya strain ofE. coli. Addition of cAMP restoredβ-galactosidase in thecya strain. The expression ofφ(glgC‘−’lacZ) encodedβ-galactosidase activity in a series ofspoT mutants exhibited an apparent exponential relationship to intracellular guanosine 5′-diphosphate 3′-diphosphate (ppGpp) levels. These results provide evidence for the control of glycogen biosynthesis in vivo by cAMP and ppGpp at the level of gene expression, and identify a region of DNA required for the control. Theφ(glgC‘−’lacZ) encodedβ-galactosidase activity was also elevated three-to five-fold in strain AC70R1, which contains a transacting mutation (glgQ) that affects the levels of the glycogen biosynthetic enzymes andglgC transcripts.


Enzyme Gene Expression Response System Diphosphate Gene Fusion 
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Copyright information

© Springer-Verlag New York Inc. 1990

Authors and Affiliations

  • Tony Romeo
    • 1
  • Jill Black
    • 1
  • Jack Preiss
    • 1
  1. 1.Department of BiochemistryMichigan State UniversityEast LansingUSA

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