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"Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I." |
Robins P, Pappin DJ, Wood RD, Lindahl T |
Published Nov. 18, 1994 in J Biol Chem volume 269 .
Pubmed ID: 7961795
Abstract:
| A nuclear 42-kDa 5'-->3'-exonuclease, DNase IV, was found previously in animal tissues. The enzyme has been purified from HeLa cells and shown to possess two catalytic properties characteristic of the 5'-nuclease function of Escherichia coli DNA polymerase I,-DNase IV removes single-stranded 5' regions from splayed-arm DNA structures by endonucleolytic incision at the bifurcation point and possesses RNase H activity. Determination of the molecular masses of tryptic and V8 peptides of DNase IV by mass spectrometry identified the enzyme as the human homolog of the Schizosaccharomyces pombe Rad2 protein. The protein sequence retains conserved residues and shows significant homology to the sequences of the 5'-nuclease domain of E. coli DNA polymerase I and related microbial enzymes. |
This publication refers to following REPAIRtoire entries:
| Genes | |
| Proteins |
Last modification of this entry: Oct. 6, 2010
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