Human placental endonuclease cleaves Holliday junctions.
A partially purified endonuclease from human placenta cleaves cruciform structures. The placental enzyme is active both on extruded cruciform structures from negatively supercoiled covalently closed circular plasmid DNA and on synthetic X-junctions formed by reannealing short oligonucleotides. Plasmids containing natural or cloned palindromes such as pBR322 and pHD101-3 were used as substrates. The synthetic X-junction tetramer DNA formed by reannealing short oligonucleotides, was converted into dimer form by the enzyme. This is the first report of an enzyme activity involved in resolution of recombination intermediates in higher eukaryotes and second report of a cellular enzyme.
Jeyaseelan
R
R
Cancer Biology Division, School of Biological Sciences, Madurai Kamaraj University, India.
Shanmugam
G
G
D004247:DNA / Q000378:metabolism*; D004269:DNA, Bacterial / Q000378:metabolism; D004278:DNA, Superhelical / Q000378:metabolism; D004720:Endonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D005260:Female; D006801:Humans; D046911:Macromolecular Substances; D010920:Placenta / Q000201:enzymology*; D010957:Plasmids; D011247:Pregnancy; D011995:Recombination, Genetic
D004269:DNA, Bacterial; D004278:DNA, Superhelical; D046911:Macromolecular Substances; D004247:DNA; D004720:Endonucleases