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Papers In Press, published online ahead of print June 19, 2002
J. Biol. Chem, 10.1074/jbc.M204268200
Submitted on May 1, 2002
Revised on June 10, 2002
Accepted on June 19, 2002
Department of Biological Chemistry, University of Copenhagen, Copenhagen K DK-1307
Corresponding Author: carstenpt{at}mermaid.molbio.ku.dk
In Escherichia coli there are two pathways for conversion of adenine into guanine nucleotides, both involving the intermediary formation of IMP. The major pathway involves conversion of adenine into hypoxanthine in three steps via adenosine and inosine, with subsequent phosphoribosylation of hypoxanthine to IMP. The minor pathway, involves formation of ATP which is converted via the histidine pathway to the purine intermediate AICAR and subsequently to IMP. Here we describe E. coli mutants, in which a third pathway for conversion of adenine to IMP has been activated. This pathway was shown to involve direct deamination of adenine to hypoxanthine by a manganese-dependent adenine deaminase encoded by a cryptic gene, yicP, which we propose be renamed ade. Insertion elements, located from -145 to +13 bp relative to the transcription start site, activated the ade gene, as did unlinked mutations in the hns gene, encoding the histone-like protein H-NS. Gene fusion analysis indicated that ade transcription is repressed more than 10-fold by H-NS, and that a region of 231 bp including the ade promoter is sufficient for this regulation. The activating insertion elements essentially eliminated the H-NS mediated silencing, and stimulated ade gene expression two to three-fold independently of the H-NS protein.
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