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Originally published In Press as doi:10.1074/jbc.M010648200 on February 27, 2001

J. Biol. Chem., Vol. 276, Issue 21, 18038-18045, May 25, 2001
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A Plant 3'-Phosphoesterase Involved in the Repair of DNA Strand Breaks Generated by Oxidative Damage*

Marco Betti, Stefania Petrucco, Angelo Bolchi, Giorgio Dieci, and Simone OttonelloDagger

From the Istituto di Scienze Biochimiche, Università di Parma, I-43100 Parma, Italy

Two novel, structurally and functionally distinct phosphatases have been identified through the functional complementation, by maize cDNAs, of an Escherichia coli diphosphonucleoside phosphatase mutant strain. The first, ZmDP1, is a classical Mg2+-dependent and Li+-sensitive diphosphonucleoside phosphatase that dephosphorylates both 3'-phosphoadenosine 5'-phosphate (3'-PAP) and 2'-PAP without any discrimination between the 3'- and 2'-positions. The other, ZmDP2, is a distinct phosphatase that also catalyzes diphosphonucleoside dephosphorylation, but with a 12-fold lower Li+ sensitivity, a strong preference for 3'-PAP, and the unique ability to utilize double-stranded DNA molecules with 3'-phosphate- or 3'-phosphoglycolate-blocking groups as substrates. Importantly, ZmDP2, but not ZmDP1, conferred resistance to a DNA repairdeficient E. coli strain against oxidative DNA-damaging agents generating 3'-phosphate- or 3'-phosphoglycolate-blocked single strand breaks. ZmDP2 shares a partial amino acid sequence similarity with a recently identified human polynucleotide kinase 3'-phosphatase that is thought to be involved in DNA repair, but is devoid of 5'-kinase activity. ZmDP2 is the first DNA 3'-phosphoesterase thus far identified in plants capable of converting 3'-blocked termini into priming sites for reparative DNA polymerization.


* This work was supported by grants from the National Research Council of Italy, Target Project on "Biotechnology," and the Ministry of University and Scientific and Technological Research (Rome, Italy).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF288075 and AF307152.

Dagger To whom correspondence should be addressed. Tel.: 39-521-905646; Fax: 39-521-905151; E-mail: s.ottonello@unipr.it.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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