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 Garges, S Articles by Adhya, S Search for Related Content PubMed PubMed Citation Articles by Garges, S Articles by Adhya, S

Next Article 

J Bacteriol. 1988 April; 170(4): 1417-1422

research-article

Cyclic AMP-induced conformational change of cyclic AMP receptor protein (CRP): intragenic suppressors of cyclic AMP-independent CRP mutations.

Developmental Genetics Section, National Cancer Institute, Bethesda, Maryland 20892.

ABSTRACT

We isolated and characterized crp mutations in Escherichia coli that allow cyclic AMP (cAMP) receptor protein to function without cAMP. These mutants defined a region involved in the cAMP-induced allosteric change of cAMP receptor protein that is necessary for activation of the protein. Currently, we have isolated intragenic suppressors of the crp mutations. These crp (Sup) mutants require cAMP for activity. The crp (Sup) mutations map in regions which define new sites of changes involved in cAMP receptor protein activation. From these results, we suggest that to activate cAMP receptor protein cAMP brings about (i) a hinge reorientation to eject the DNA-binding F alpha-helices, (ii) proper alignment between the two subunits, and (iii) an adjustment between the position of the two domains. Cyclic GMP fails to effect the last step.

This article has been cited by other articles:

• Doern, C. D., Holder, R. C., Reid, S. D. (2008). Point mutations within the streptococcal regulator of virulence (Srv) alter protein-DNA interactions and Srv function. Microbiology 154: 1998-2007 [Abstract] [Full Text]  
• Youn, H., Koh, J., Roberts, G. P. (2008). Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli. J. Bacteriol. 190: 4532-4540 [Abstract] [Full Text]  
• Youn, H., Kerby, R. L., Conrad, M., Roberts, G. P. (2006). Study of Highly Constitutively Active Mutants Suggests How cAMP Activates cAMP Receptor Protein. J. Biol. Chem. 281: 1119-1127 [Abstract] [Full Text]  
• Mueller, K. J., Freitag, N. E. (2005). Pleiotropic Enhancement of Bacterial Pathogenesis Resulting from the Constitutive Activation of the Listeria monocytogenes Regulatory Factor PrfA. Infect. Immun. 73: 1917-1926 [Abstract] [Full Text]  
• Wong, K. K. Y., Freitag, N. E. (2004). A Novel Mutation within the Central Listeria monocytogenes Regulator PrfA That Results in Constitutive Expression of Virulence Gene Products. J. Bacteriol. 186: 6265-6276 [Abstract] [Full Text]  
• Malecki, J., Polit, A., Wasylewski, Z. (2000). Kinetic Studies of cAMP-induced Allosteric Changes in Cyclic AMP Receptor Protein from Escherichia coli. J. Biol. Chem. 275: 8480-8486 [Abstract] [Full Text]  
• Shi, Y., Wang, S., Krueger, S., Schwarz, F. P. (1999). Effect of Mutations at the Monomer-Monomer Interface of cAMP Receptor Protein on Specific DNA Binding. J. Biol. Chem. 274: 6946-6956 [Abstract] [Full Text]  
• Vega, Y., Dickneite, C., Ripio, M.-T., Böckmann, R., González-Zorn, B., Novella, S., Domínguez-Bernal, G., Goebel, W., Vázquez-Boland, J. A. (1998). Functional Similarities between the Listeria monocytogenes Virulence Regulator PrfA and Cyclic AMP Receptor Protein: the PrfA* (Gly145Ser) Mutation Increases Binding Affinity for Target DNA. J. Bacteriol. 180: 6655-6660 [Abstract] [Full Text]  
• Krueger, S., Gorshkova, I., Brown, J., Hoskins, J., McKenney, K. H., Schwarz, F. P. (1998). Determination of the Conformations of cAMP Receptor Protein and Its T127L,S128A Mutant with and without cAMP from Small Angle Neutron Scattering Measurements. J. Biol. Chem. 273: 20001-20006 [Abstract] [Full Text]  
• Lazazzera, B A, Bates, D M, Kiley, P J (1993). The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state.. Genes Dev. 7: 1993-2005 [Abstract]