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J. Biol. Chem., Vol. 276, Issue 21, 18038-18045, May 25, 2001
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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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF288075 and AF307152.
A Plant 3'-Phosphoesterase Involved in the Repair of DNA Strand
Breaks Generated by Oxidative Damage*
*
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.
To whom correspondence should be addressed. Tel.: 39-521-905646;
Fax: 39-521-905151; E-mail: s.ottonello@unipr.it.
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