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Molecular & Cellular Proteomics 1:179-183, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

The Rickettsia prowazekii Invasion Gene Homolog (invA) Encodes a Nudix Hydrolase Active on Adenosine (5')-pentaphospho-(5')-adenosine^*

Jariyanart Gaywee, WenLian Xu, Suzana Radulovic, Maurice J. Bessman and Abdu F. Azad^,¶

Department of Microbiology and Immunology, School of Medicine, University of Maryland, Baltimore, Maryland 21201
Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218

The genomic sequence of Rickettsia prowazekii, the obligate intracellular bacterium responsible for epidemic typhus, reveals an uncharacterized invasion gene homolog (invA). The deduced protein of 18,752 Da contains a Nudix signature, the specific motif found in the Nudix hydrolase family. To characterize the function of InvA, the gene was cloned and overexpressed in Escherichia coli. The expressed protein was purified to near homogeneity and subsequently tested for its enzymatic activity against a series of nucleoside diphosphate derivatives. The purified InvA exhibits hydrolytic activity toward dinucleoside oligophosphates (Np_nN; n 5), a group of cellular signaling molecules. At optimal pH 8.5, the enzyme actively degrades adenosine (5')-pentaphospho-(5')-adenosine into ATP and ADP with a K_m of 0.1 mM and k_cat of 1.9 s^-1. Guanosine (5')-pentaphospho-(5')-guanosine and adenosine-(5')-hexaphospho (5')-adenosine are also substrates. Similar to other Nudix hydrolases, InvA requires a divalent metal cation, Mg²⁺ or Zn²⁺, for optimal activity. These data suggest that the rickettsial invasion protein likely plays a role in controlling the concentration of stress-induced dinucleoside oligophosphates following bacterial invasion.

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