Holliday junction cleavage by yeast Rad1 protein

in Nature (1994), 371

Yeast excision repair RAD2 encodes a single-stranded DNA endonuclease

in Nature (1993), 366

The formation and enzymatic repair of DNA modifications caused by haloethylnitrosoureas and related compounds

in Nucleic Acids Symposium Series (1992), 105

Excision of imidazole ring-opened N7-hydroxyethylguanine from chloroethylnitrosourea-treated DNA by Escherichia coli formamidopyrimidine-DNA glycolsylase

in IARC Scientific Publications (1991), 105

Release of 7-alkylguanines from N-(2-chloroethyl)-N'-cyclohexyl-N-nitrosourea-modified DNA by 3 methyladenine DNA glycosylase

in Cancer Research (1991), 51

Development of monoclonal antibodies recognizing 7-(2-hydroxyethyl)guanine and imidazole ring-opened 7-(2-hydroxyethyl)guanine.

in Carcinogenesis (1990), 11

Release of the chloroethyl ethyl sulfide-modified DNA bases by bacterial 3-methyladenine DNA glycosylase I and II

in Carcinogenesis (1989), 10(3), 489-492

Further Purification and Characterization of the DNA 3'-Phosphatase from Rat-Liver Chromatin Which Is Also a Polynucleotide 5'-Hydroxyl Kinase

in European Journal of Biochemistry (1988), 171(1-2), 59-66

The DNA 3'-phosphatase activity of rat-liver chromatin has been purified. A DNA 5'-hydroxyl kinase activity comigrates at each step of purification. Both enzymes have the same molecular mass (79 kDa) and ... [more ▼]

The DNA 3'-phosphatase activity of rat-liver chromatin has been purified. A DNA 5'-hydroxyl kinase activity comigrates at each step of purification. Both enzymes have the same molecular mass (79 kDa) and the same isoelectric point (8.6). It thus seems that the two activities are born by the same protein just as with the phage T4 enzyme which is, at the same time, a 5'-hydroxyl kinase and a 3'-phosphatase. An additional argument is that ATP, which does not influence the rate of the 3'-phosphatase reaction but which is a cosubstrate of the 5'-hydroxyl kinase, protects the 3'-phosphatase activity against thermal denaturation and trypsin digestion. The two active sites must, however, be largely independent within a common support: the thermal denaturation and trypsin inactivation rates are very different for the two activities; increasing the ionic strength activates the kinase and inhibits the phosphatase; polyvalent anions inhibit the phosphatase and have little effect on the kinase. The two active sites might belong to different domains of the protein; they could not however be separated by a partial trypsin digestion. The rates of 3'-dephosphorylation and 5'-phosphorylation by the chromatin enzyme are the same in native and denatured DNA. The 3'-phosphatase has no action on 3'-monodeoxynucleotide, but it hydrolyzes the 3'-phosphate in dinucleotides. The Km of the 3'-phosphatase is 0.548 microM. The Km (5'-OH) and Km (ATP) of the 5'-hydroxyl kinase are about 3.9 microM and 0.69 microM respectively. The chromatin enzyme is unable to hydrolyze 3'-phosphoglycolate ends in DNA. [less ▲]

3' phosphatase chromatinienne et réparation des cassures produites dans l'ADN par les radiations ionisantes

Doctoral thesis (1986)

The DNA 3'-phosphatase and 5'-hydroxyl kinase of rat liver chromatin

in FEBS Letters (1983), 160(1,2), 46-50