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Endonuclease II of Escherichia coli is exonuclease III.
Open accessAbstract
Exonuclease III, a phosphatase-exonuclease specific for bihelical DNA, wn the preparation was endonuclease II, an activity specific for DNA that has been partially depurinated by treatment with methyl methanesulfonate. The two activities, which could not be separated by electrophoresis, by sedimentation, or by gel filtration, were associated with a single monomeric protein of 28,000 daltons. To explain how a relatively small protein could have such diverse activities, it is proposed that one site on the enzyme can recognize interstrand spaces created either by depurination or by spontaneous terminal unwinding of a DNA duplex.
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Cited by
Human L1 retrotransposon encodes a conserved endonuclease required for retrotransposition
Feng, Q., Moran, J. V., Kazazian, H. H., & Boeke, J. D. (1996) · Cell · doi:10.1016/s0092-8674(00)81997-2 · Cited by 1,139
DNA Glycosylases, Endonucleases for Apurinic/Apyrimidinic Sites, and Base Excision-Repair
Lindahl, T. (1979) · Progress in Nucleic Acid Research and Molecular Biology · doi:10.1016/s0079-6603(08)60800-4 · Cited by 554
Demple, B., Herman, T., & Chen, D. S. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11450 · Cited by 537
DNA N-glycosidases: properties of uracil-DNA glycosidase from Escherichia coli.
Lindahl, T., Ljungquist, S., Siegert, W., Nyberg, B., & Sperens, B. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40386-3 · Cited by 522
The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA
Wilson, D. M., & Barsky, D. (2001) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(01)00063-5 · Cited by 408
Metadata
- Authors
- Weiss, B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1976-04
- Volume
- 251
- Issue
- 7
- Pages
- 1896-1901
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1508028184
- Cited by
- 198
- References
- 0
- FWCI
- 4.77
- Type
- journal article
- Language
- en
- Open access
- hybrid
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