CAP (catabolite activator protein)

2012 ◽  
Keyword(s):  
Catabolite Activator Protein ◽  
Activator Protein

scholarly journals The Transcriptional Factors MurR and Catabolite Activator Protein Regulate N-Acetylmuramic Acid Catabolism in Escherichia coli

2008 ◽  
Vol 190 (20) ◽  
pp. 6598-6608 ◽  
Author(s):  
Tina Jaeger ◽  
Christoph Mayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Sole Source ◽  
Lag Phase ◽  
Face To Face ◽  
E Coli ◽  
Catabolite Activator Protein ◽  
Activator Protein ◽  
High Level ◽  
First Time

ABSTRACT The MurNAc etherase MurQ of Escherichia coli is essential for the catabolism of the bacterial cell wall sugar N-acetylmuramic acid (MurNAc) obtained either from the environment or from the endogenous cell wall (i.e., recycling). High-level expression of murQ is required for growth on MurNAc as the sole source of carbon and energy, whereas constitutive low-level expression of murQ is sufficient for the recycling of peptidoglycan fragments continuously released from the cell wall during growth of the bacteria. Here we characterize for the first time the expression of murQ and its regulation by MurR, a member of the poorly characterized RpiR/AlsR family of transcriptional regulators. Deleting murR abolished the extensive lag phase observed for E. coli grown on MurNAc and enhanced murQ transcription some 20-fold. MurR forms a stable multimer (most likely a tetramer) and binds to two adjacent inverted repeats within an operator region. In this way MurR represses transcription from the murQ promoter and also interferes with its own transcription. MurNAc-6-phosphate, the substrate of MurQ, was identified as a specific inducer that weakens binding of MurR to the operator. Moreover, murQ transcription depends on the activation by cyclic AMP (cAMP)-catabolite activator protein (CAP) bound to a class I site upstream of the murQ promoter. murR and murQ are divergently orientated and expressed from nonoverlapping face-to-face (convergent) promoters, yielding transcripts that are complementary at their 5′ ends. As a consequence of this unusual promoter arrangement, cAMP-CAP also affects murR transcription, presumably by acting as a roadblock for RNA polymerase.

Mutants with substitutions for Glu171 in the catabolite activator protein (CAP) of Escherichia coli activate transcription from the lac promoter

1993 ◽  
Vol 238-238 (1-2) ◽  
pp. 155-160 ◽  
Author(s):  
Astrid Breul ◽  
Heike Aßmann ◽  
Regina Golz ◽  
Brigitte von Wilcken-Bergmann ◽  
Benno Müller-Hill
Keyword(s):  
Escherichia Coli ◽  
Catabolite Activator Protein ◽  
Activator Protein ◽  
Lac Promoter

scholarly journals Catabolite activator protein: DNA binding and transcription activation

2004 ◽  
Vol 14 (1) ◽  
pp. 10-20 ◽  
Author(s):  
Catherine L Lawson ◽  
David Swigon ◽  
Katsuhiko S Murakami ◽  
Seth A Darst ◽  
Helen M Berman ◽  
...  
Keyword(s):  
Dna Binding ◽  
Transcription Activation ◽  
Catabolite Activator Protein ◽  
Activator Protein

scholarly journals Structure of catabolite activator protein with cobalt(II) and sulfate

2014 ◽  
Vol 70 (5) ◽  
pp. 560-563 ◽  
Author(s):  
Ramya R. Rao ◽  
Catherine L. Lawson
Keyword(s):  
Transcription Activation ◽  
Complex Structures ◽  
Catabolite Activator Protein ◽  
Activator Protein ◽  
Terminal Domain ◽  
Dna Backbone ◽  
Cobalt Binding ◽  
Binding Residues ◽  
Dna Complex ◽  
Crystal Contact

The crystal structure of cyclic AMP–catabolite activator protein (CAP) fromEscherichia colicontaining cobalt(II) chloride and ammonium sulfate is reported at 1.97 Å resolution. Each of the two CAP subunits in the asymmetric unit binds one cobalt(II) ion, in each case coordinated by N-terminal domain residues His19, His21 and Glu96 plus an additional acidic residue contributedviaa crystal contact. The three identified N-terminal domain cobalt-binding residues are part of a region of CAP that is important for transcription activation at class II CAP-dependent promoters. Sulfate anions mediate additional crystal lattice contacts and occupy sites corresponding to DNA backbone phosphate positions in CAP–DNA complex structures.

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