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J Biol Chem, Vol. 275, Issue 7, 5120-5123, February 18, 2000
From the Laboratory of Molecular Genetics, Leiden Institute of
Chemistry, Gorlaeus Laboratories, Leiden University, Einsteinweg 55, P.O. Box 9502, 2300 RA Leiden, The Netherlands
Nucleotide excision repair in Escherichia
coli is a multistep process in which DNA damage is removed by
incision of the DNA on both sides of the damage, followed by removal of
the oligonucleotide containing the lesion. The two incision reactions
take place in a complex of damaged DNA with UvrB and UvrC. It has been
shown (Lin, J.-J., and Sancar, A. (1992) J. Biol.
Chem. 267, 17688-17692) that the catalytic site for incision on
the 5' side of the damage is located in the UvrC protein. Here we show
that the catalytic site for incision on the 3' side is in this protein
as well, because substitution R42A abolishes 3' incision, whereas
formation of the UvrBC-DNA complex and the 5' incision reaction are
unaffected. Arg42 is part of a region that is homologous to
the catalytic domain of the homing endonuclease I-TevI. We
propose that the UvrC protein consists of two functional parts, with
the N-terminal half for the 3' incision reaction and the C-terminal
half containing all the determinants for the 5' incision reaction.
Catalytic Sites for 3' and 5' Incision of Escherichia
coli Nucleotide Excision Repair Are Both Located in UvrC*
*
This work was supported by the J. A. Cohen Institute for
Radiopathology and Radiation Protection and a European Community Structural Biology Framework IV Program grant.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.: 0-715274773;
Fax: 0-715274537; E-mail: N.Goosen@chem.Leidenuniv.nl.
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