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Originally published In Press as doi:10.1074/jbc.M908725199 on March 10, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16366-16372, May 26, 2000
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Dissection of the Functional Domains of the Leishmania Surface Membrane 3'-Nucleotidase/Nuclease, a Unique Member of the Class I Nuclease Family*

Alain DebrabantDagger , Elodie Ghedin§, and Dennis M. Dwyer

From the Cell Biology Section, Laboratory of Parasitic Diseases, Division of Intramural Research, NIAID, National Institutes of Health, Bethesda, Maryland 20892-0425

Class I nucleases are a family of enzymes that specifically hydrolyze single-stranded nucleic acids. Recently, we characterized the gene encoding a new member of this family, the 3'-nucleotidase/nuclease (Ld3'NT/NU) of the parasitic protozoan Leishmania donovani. The Ld3'NT/NU is unique as it is the only class I nuclease that is a cell surface membrane-anchored protein. Currently, we used a homologous episomal expression system to dissect the functional domains of the Ld3'NT/NU. Our results showed that its N-terminal signal peptide targeted this protein into the endoplasmic reticulum. Using Ld3'NT/NU-green fluorescent protein chimeras, we showed that the C-terminal domain of the Ld3'NT/NU functioned to anchor this protein into the parasite cell surface membrane. Further, removal of the Ld3'NT/NU C-terminal domain resulted in its release/secretion as a fully active enzyme. Moreover, deletion of its single N-linked glycosylation site showed that such glycosylation was not required for the enzymatic functions of the Ld3'NT/NU. Thus, using the fidelity of a homologous expression system, we have defined some of the functional domains of this unique member of the class I nuclease family.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger National Institutes of Health Visiting Associate. Supported by a postdoctoral fellowship from the Fogarty International Center and the NIAID, National Institutes of Health. Present address: Laboratory of Parasite Biology and Biochemistry, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892.

§ National Institutes of Health Visiting Fellow. Supported by a postdoctoral fellowship from the Fogarty International Center and the NIAID, National Institutes of Health.

To whom correspondence should be addressed: NIAID, National Institutes of Health, LPD, Bldg. 4, Rm. 126, 4 Center Dr. MSC 0425, Bethesda, MD 20892-0425. Tel.: 301-496-5969; Fax: 301-402-2201; E-mail: ddwyer@niaid.nih.gov.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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