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Papers In Press, published online ahead of print January 9, 2006
J. Biol. Chem, 10.1074/jbc.M512672200
Submitted on November 28, 2005
Revised on January 6, 2006
Accepted on January 9, 2006
Laboratory of Cell Biology, NHLBI, Bethesda, MD 20892-8017
Corresponding Author: peterkofsky{at}nih.gov
A widely accepted model for catabolite repression posits that phospho-IIAGlc of the bacterial phosphotransferase system (PTS) activates adenylyl cyclase (AC) activity. Attempts over many years to observe such regulatory properties of AC in vitro had been unsuccessful. To further study the regulation, AC was produced fused to the transmembrane segments of the serine chemoreceptor, Tsr. Cells harboring Tsr-AC and normal AC, expressed from the cya promoter on a low copy-number vector, exhibit similar behavior with respect to elevation of cAMP levels resulting from deletion of crp, expressing the catabolite regulatory protein. Membrane-bound Tsr-AC exhibits activity comparable to the native form of AC. Tsr-AC binds IIAGlc specifically, regardless of its phosphorylation state, but not the two general PTS proteins, enzyme I and HPr; IIAGlc binding is localized to the C-terminal region of AC. Binding to membranes of either dephospho- or phospho-IIAGlc has no effect on AC activity. However, in the presence of an E. coli extract, P-IIAGlc, but not IIAGlc, stimulates AC activity. Based on these findings of a direct interaction of IIAGlc with AC, but activity regulation only in the presence of E. coli extract, a revised model for AC activity regulation is proposed.
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