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

research-article

Escherichia coli cyclic AMP receptor protein mutants provide evidence for ligand contacts important in activation.

Center for Advanced Research in Biotechnology, Maryland Biotechnology Institute, Rockville.

ABSTRACT

The three-dimensional model of the Escherichia coli cyclic AMP (cAMP) receptor protein (CRP) shows that several amino acids are involved as chemical contacts for binding cAMP. We have constructed and characterized mutants at four of these positions, E72, R82, S83, and R123. The mutations were made in wild-type crp as well as a cAMP-independent crp, crp*. The activities of the mutant proteins were characterized in vivo for their ability to activate the lac operon. These results provide genetic evidence to support that E72 and R82 are essential and S83 and R123 are important in the activation of CRP by cAMP.

This article has been cited by other articles:

• Youn, H., Kerby, R. L., Koh, J., Roberts, G. P. (2007). A C-helix Residue, Arg-123, Has Important Roles in Both the Active and Inactive Forms of the cAMP Receptor Protein. J. Biol. Chem. 282: 3632-3639 [Abstract] [Full Text]  
• Balsalobre, C., Johansson, J., Uhlin, B. E. (2006). Cyclic AMP-Dependent Osmoregulation of crp Gene Expression in Escherichia coli.. J. Bacteriol. 188: 5935-5944 [Abstract] [Full Text]  
• Lee, Y.-Y., Shearer, N., Spiro, S. (2006). Transcription factor NNR from Paracoccus denitrificans is a sensor of both nitric oxide and oxygen: isolation of nnr* alleles encoding effector-independent proteins and evidence for a haem-based sensing mechanism.. Microbiology 152: 1461-1470 [Abstract] [Full Text]  
• Chen, R., Lee, J. C. (2003). Functional Roles of Loops 3 and 4 in the Cyclic Nucleotide Binding Domain of Cyclic AMP Receptor Protein from Escherichia coli. J. Biol. Chem. 278: 13235-13243 [Abstract] [Full Text]  
• Herrero, A., Muro-Pastor, A. M., Flores, E. (2001). Nitrogen Control in Cyanobacteria. J. Bacteriol. 183: 411-425 [Full Text]  
• Ochoa de Alda, J. A. G., Houmard, J. (2000). Genomic survey of cAMP and cGMP signalling components in the cyanobacterium Synechocystis PCC 6803. Microbiology 146: 3183-3194 [Abstract] [Full Text]  
• Tibbs, G. R., Liu, D. T., Leypold, B. G., Siegelbaum, S. A. (1998). A State-independent Interaction between Ligand and a Conserved Arginine Residue in Cyclic Nucleotide-gated Channels Reveals a Functional Polarity of the Cyclic Nucleotide Binding Site. J. Biol. Chem. 273: 4497-4505 [Abstract] [Full Text]  
• Passner, J. M., Steitz, T. A. (1997). The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proc. Natl. Acad. Sci. USA 94: 2843-2847 [Abstract] [Full Text]  
• Moore, J. L., Gorshkova, I. I., Brown, J. W., McKenney, K. H., Schwarz, F. P. (1996). Effect of cAMP Binding Site Mutations on the Interaction of cAMP Receptor Protein with Cyclic Nucleoside Monophosphate Ligands and DNA. J. Biol. Chem. 271: 21273-21278 [Abstract] [Full Text]  
• Gorshkova, I., Moore, J. L., McKenney, K. H., Schwarz, F. P. (1995). Thermodynamics of Cyclic Nucleotide Binding to the cAMP Receptor Protein and Its T127L Mutant. J. Biol. Chem. 270: 21679-21683 [Abstract] [Full Text]