The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Purification and Properties of the recBC DNase of Escherichia coli K-12
Open accessAbstract
Abstract The deoxyribonuclease controlled by the recB and recC loci of Escherichia coli K-12 has been purified to near homogeneity. It is composed of two nonidentical polypeptide chains with a combined molecular weight of approximately 270,000. In the presence of ATP the enzyme hydrolyzes linear duplex or single stranded DNA in an exonucleolytic manner to 5'-phosphoryl-terminated oligonucleotides of an average length of 4.5. The enzyme can also cleave single stranded DNA endonucleolytically, being stimulated 7-fold by ATP in this reaction. However, no nuclease activity is observed on closed circular duplex DNA. In the course of exonuclease digestion more than 20 ATP molecules are hydrolyzed to ADP and inorganic phosphate for each DNA phosphodiester bond broken. There is no ATP hydrolysis in the absence of degradable DNA.
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Cites
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Cited by
Biochemistry of homologous recombination in Escherichia coli
Kowalczykowski, S. C., Dixon, D. A., Eggleston, A. K., Lauder, S. D., & Rehrauer, W. M. (1994) · Microbiological Reviews · doi:10.1128/mr.58.3.401-465.1994 · Cited by 1,250
RecBCD Enzyme and the Repair of Double-Stranded DNA Breaks
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Horii, Z.-I., & Clark, A. J. (1973) · Journal of Molecular Biology · doi:10.1016/0022-2836(73)90176-9 · Cited by 484
Collapse and repair of replication forks in Escherichia coli
Kuzminov, A. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.tb02403.x · Cited by 364
Degradation of DNA RNA Hybrids by Ribonuclease H and DNA Polymerases of Cellular and Viral Origin
Keller, W., & Crouch, R. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.11.3360 · Cited by 222
Metadata
- Authors
- Goldmark, P. J., & Linn, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1972-03
- Volume
- 247
- Issue
- 6
- Pages
- 1849-1860
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1533085219
- Cited by
- 321
- References
- 17
- FWCI
- 15.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
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