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J Biol Chem, Vol. 274, Issue 3, 1203-1206, January 15, 1999

COMMUNICATION
The Gene, ialA, Associated with the Invasion of Human Erythrocytes by Bartonella bacilliformis, Designates a Nudix Hydrolase Active on Dinucleoside 5'-Polyphosphates

G. Bernard Conyers and Maurice J. Bessman^¶

From the ^¶ Department of Biology and the  McCollum-Pratt Institute and the  Department of Biophysics, The Johns Hopkins University, Baltimore, Maryland 21218

ialA, one of two genes associated with the invasion of human red blood cells by Bartonella bacilliformis, the causative agent of several diseases, has been cloned and expressed in Escherichia coli. The protein, IalA, contains an amino acid array characteristic of a family of enzymes, the Nudix hydrolases, active on a variety of nucleoside diphosphate derivatives. IalA has been purified, identified, and characterized as an enzyme catalyzing the hydrolysis of members of a class of signaling nucleotides, the dinucleoside polyphosphates, with its highest activity on adenosine 5'-tetraphospho-5'-adenosine (Ap₄A), but also hydrolyzing Ap₅A, Ap₆A, Gp₄G, and Gp₅G. In each case, a pyrophosphate linkage is cleaved yielding a nucleoside triphosphate and the remaining nucleotide moiety.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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