Robins, P., Pappin, D. J., Wood, R. D., Lindahl, T. (November 1994) Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I. J Biol Chem, 269 (46). pp. 28535-8. ISSN 0021-9258 (Print)0021-9258 (Linking)
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.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Amino Acid Sequence DNA Polymerase I/ chemistry/metabolism DNA-Binding Proteins Endodeoxyribonucleases Escherichia coli/ enzymology Exodeoxyribonucleases/ chemistry/isolation & purification/metabolism Flap Endonucleases Fungal Proteins/chemistry HeLa Cells Humans Molecular Sequence Data Saccharomyces cerevisiae Proteins Schizosaccharomyces/metabolism Sequence Homology, Amino Acid |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > DNA polymerase organism description > bacteria > escherichia coli |
| CSHL Authors: | |
| Communities: | CSHL labs > Pappin lab |
| Depositing User: | Matt Covey |
| Date: | 18 November 1994 |
| Date Deposited: | 11 Sep 2014 15:00 |
| Last Modified: | 11 Sep 2014 15:00 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/30783 |
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