This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhang, X.
Right arrow Articles by Schleif, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, X.
Right arrow Articles by Schleif, R.

Next Article 

J. Bacteriol., Jan 1998, 195-200, Vol 180, No. 2
Copyright © 1998, American Society for Microbiology

Catabolite gene activator protein mutations affecting activity of the araBAD promoter [In Process Citation]

X Zhang and R Schleif
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.

We have studied catabolite gene activator protein (CAP) activation at the araBAD promoter, pBAD, in the absence of DNA looping. We ruled out the two most plausible indirect activation mechanisms: CAP-induced folding of upstream DNA back upon RNA polymerase, and CAP-induced stabilization of AraC binding to DNA. Therefore, a direct CAP-RNA polymerase interaction seemed likely. We sought and found CAP mutants defective in transcription activation at pBAD that retained normal DNA binding affinity. Some mutations altered residues in the interval from positions 150 to 164 that includes CAP activating region 1 (AR1), which has been shown to contact RNA polymerase at a number of promoters. Unexpectedly, additional mutations were found that altered residues in the region between positions 46 and 68 and at position 133. This includes the region known as activating region 3 (AR3). Mutations from both groups also affect the araFGH and rhaBAD promoters.


This article has been cited by other articles:

  • Buchan, A., Ornston, L. N. (2005). When Coupled to Natural Transformation in Acinetobacter sp. Strain ADP1, PCR Mutagenesis Is Made Less Random by Mismatch Repair. Appl. Environ. Microbiol. 71: 7610-7612 [Abstract] [Full Text]  
  • Wickstrum, J. R., Santangelo, T. J., Egan, S. M. (2005). Cyclic AMP Receptor Protein and RhaR Synergistically Activate Transcription from the L-Rhamnose-Responsive rhaSR Promoter in Escherichia coli. J. Bacteriol. 187: 6708-6718 [Abstract] [Full Text]  
  • Ruiz, R., Marques, S., Ramos, J. L. (2003). Leucines 193 and 194 at the N-Terminal Domain of the XylS Protein, the Positive Transcriptional Regulator of the TOL meta-Cleavage Pathway, Are Involved in Dimerization. J. Bacteriol. 185: 3036-3041 [Abstract] [Full Text]  
  • Howard, V. J., Belyaeva, T. A., Busby, S. J. W., Hyde, E. I. (2002). DNA binding of the transcription activator protein MelR from Escherichia coli and its C-terminal domain. Nucleic Acids Res 30: 2692-2700 [Abstract] [Full Text]  
  • Holcroft, C. C., Egan, S. M. (2000). Interdependence of Activation at rhaSR by Cyclic AMP Receptor Protein, the RNA Polymerase Alpha Subunit C-Terminal Domain, and RhaR. J. Bacteriol. 182: 6774-6782 [Abstract] [Full Text]  
  • Dhiman, A., Schleif, R. (2000). Recognition of Overlapping Nucleotides by AraC and the Sigma Subunit of RNA Polymerase. J. Bacteriol. 182: 5076-5081 [Abstract] [Full Text]  
  • Holcroft, C. C., Egan, S. M. (2000). Roles of Cyclic AMP Receptor Protein and the Carboxyl-Terminal Domain of the alpha Subunit in Transcription Activation of the Escherichia coli rhaBAD Operon. J. Bacteriol. 182: 3529-3535 [Abstract] [Full Text]  
  • Wonderling, L. D., Stauffer, G. V. (1999). The Cyclic AMP Receptor Protein Is Dependent on GcvA for Regulation of the gcv Operon. J. Bacteriol. 181: 1912-1919 [Abstract] [Full Text]  
  • Saviola, B., Seabold, R. R., Schleif, R. F. (1998). DNA Bending by AraC: a Negative Mutant. J. Bacteriol. 180: 4227-4232 [Abstract] [Full Text]