Abstract
Eight different mutations in Haemophilus influenzae leading to deficiency in adenosine 5'-triphosphate (ATP)-dependent nuclease have been investigated in strains in which the mutations of the originally mutagenized strains have been transferred into the wild type. Sensitivity to mitomycin C and deoxycholate and complementation between extracts and deoxyribonucleic acid (DNA)-dependent ATPase activity have been measured. Genetic crosses have provided information on the relative position of the mutations on the genome. There are three complementation groups, corresponding to three genetic groups. The strains most sensitive to mitomycin and deoxycholate, derived from mutants originally selected on the basis of sensitivity to mitomycin C or methyl methanesulfonate, are in one group. Apparently all these sensitive strains lack DNA-dependent ATPase activity, as does a strain intermediate in sensitivity to deoxycholate, which is the sole representative of another group. There are four strains that are relatively resistant to deoxycholate and mitomycin C, and all of these contain the ATPase activity. Three of these are in the same genetic and complementation group, whereas the other incongruously belongs in the same group as the sensitive strains. It is postulated that there are three cistrons in H. influenzae that code for the three known subunits of the ATP-dependent nuclease.
Full text
PDF






Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Barbour S. D., Clark A. J. Biochemical and genetic studies of recombination proficiency in Escherichia coli. I. Enzymatic activity associated with recB+ and recC+ genes. Proc Natl Acad Sci U S A. 1970 Apr;65(4):955–961. doi: 10.1073/pnas.65.4.955. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chestukhin A. V., Shemyakin M. F., Kalinina N. A., Prozorov A. A. Some properties of ATP dependent deoxyribonucleases from normal and rec-mutant strains of Bacillus subtilis. FEBS Lett. 1972 Jul 15;24(1):121–125. doi: 10.1016/0014-5793(72)80841-x. [DOI] [PubMed] [Google Scholar]
- Clark A. J. Recombination deficient mutants of E. coli and other bacteria. Annu Rev Genet. 1973;7:67–86. doi: 10.1146/annurev.ge.07.120173.000435. [DOI] [PubMed] [Google Scholar]
- Doly J., Sasarman E., Anagnostopoulos C. ATP-dependent deoxyribonuclease in Bacillus subtilis and a mutant deficient in this activity. Mutat Res. 1974 Jan;22(1):15–23. doi: 10.1016/0027-5107(74)90003-7. [DOI] [PubMed] [Google Scholar]
- Emmerson P. T. Recombination deficient mutants of Escherichia coli K12 that map between thy A and argA. Genetics. 1968 Sep;60(1):19–30. doi: 10.1093/genetics/60.1.19. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Friedman E. A., Smith H. O. An adenosine triphosphate-dependent deoxyribonuclease from Hemophilus influenzae Rd. I. Purification and properties of the enzyme. J Biol Chem. 1972 May 10;247(9):2846–2853. [PubMed] [Google Scholar]
- Goldmark P. J., Linn S. Purification and properties of the recBC DNase of Escherichia coli K-12. J Biol Chem. 1972 Mar 25;247(6):1849–1860. [PubMed] [Google Scholar]
- Greth M. L., Chevallier M. R. Studies on ATP-dependent deoxyribonuclease of Haemophilus influenzae: involvement of the enzyme in the transformation process. Biochem Biophys Res Commun. 1973 Sep 5;54(1):1–8. doi: 10.1016/0006-291x(73)90880-2. [DOI] [PubMed] [Google Scholar]
- Howard-Flanders P., Theriot L. Mutants of Escherichia coli K-12 defective in DNA repair and in genetic recombination. Genetics. 1966 Jun;53(6):1137–1150. doi: 10.1093/genetics/53.6.1137. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Lieberman R. P., Oishi M. The recBC deoxyribonuclease of Escherichia coli: isolation and characterization of the subunit proteins and reconstitution of the enzyme. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4816–4820. doi: 10.1073/pnas.71.12.4816. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Notani N., Goodgal S. H. On the nature of recombinants formed during transformation in Hemophilus influenzae. J Gen Physiol. 1966 Jul;49(6):197–209. doi: 10.1085/jgp.49.6.197. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Oishi M. An ATP-dependent deoxyribonuclease from Escherichia coli with a possible role in genetic recombination. Proc Natl Acad Sci U S A. 1969 Dec;64(4):1292–1299. doi: 10.1073/pnas.64.4.1292. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Setlow J. K., Boling M. E., Beattie K. L., Kimball R. F. A complex of recombination and repair genes in Haemophilus influenzae. J Mol Biol. 1972 Jul 21;68(2):361–378. doi: 10.1016/0022-2836(72)90218-5. [DOI] [PubMed] [Google Scholar]
- Small G. D., Setlow J. K., Kooistra J., Shapanka R. Lethal effect of mitomycin C on Haemophilus influenzae. J Bacteriol. 1976 Feb;125(2):643–654. doi: 10.1128/jb.125.2.643-654.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Steinhart W. L., Herriott R. M. Fate of recipient deoxyribonucleic acid during transformation in Haemophilus influenzae. J Bacteriol. 1968 Nov;96(5):1718–1724. doi: 10.1128/jb.96.5.1718-1724.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vovis G. F., Buttin G. An ATP-dependent deoxyribonuclease from Diplococcus pneumoniae. II. Evidence for its involvement in bacterial recombination. Biochim Biophys Acta. 1970 Nov 12;224(1):42–54. [PubMed] [Google Scholar]
- Wilcox K. W., Smith H. O. Isolation and characterization of mutants of Haemophilus influenzae deficient in an adenosine 5'-triphosphate-dependent deoxyribonuclease activity. J Bacteriol. 1975 May;122(2):443–453. doi: 10.1128/jb.122.2.443-453.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- van de Putte P., Zwenk H., Rörsch A. Properties of four mutants of Escherichia coli defective in genetic recombination. Mutat Res. 1966 Oct;3(5):381–392. doi: 10.1016/0027-5107(66)90048-0. [DOI] [PubMed] [Google Scholar]
