Abstract
Caulobacter crescentus is one of a small number of bacterial species that contain a periplasmic copper-zinc superoxide dismutase (CuZnSOD). A C. crescentus mutant, with the CuZnSOD gene interrupted by a promoterless cat gene, was constructed and characterized to analyze CuZnSOD function. Periplasmic SOD does not protect against oxyradical damage in the cytosol or play a major role in maintaining the integrity of the cell envelope. Studies of the effect of sodium citrate on plating efficiency suggest that CuZnSOD protects a periplasmic or membrane function(s) requiring magnesium or calcium.
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- Ameyama M., Matsushita K., Shinagawa E., Adachi O. Biochemical and physiological functions of pyrroloquinoline quinone. Vitam Horm. 1991;46:229–270. doi: 10.1016/s0083-6729(08)60685-8. [DOI] [PubMed] [Google Scholar]
- Bannister J. V., Bannister W. H., Rotilio G. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit Rev Biochem. 1987;22(2):111–180. doi: 10.3109/10409238709083738. [DOI] [PubMed] [Google Scholar]
- Beaman L., Beaman B. L. Monoclonal antibodies demonstrate that superoxide dismutase contributes to protection of Nocardia asteroides within the intact host. Infect Immun. 1990 Sep;58(9):3122–3128. doi: 10.1128/iai.58.9.3122-3128.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Beck B. L., Tabatabai L. B., Mayfield J. E. A protein isolated from Brucella abortus is a Cu-Zn superoxide dismutase. Biochemistry. 1990 Jan 16;29(2):372–376. doi: 10.1021/bi00454a010. [DOI] [PubMed] [Google Scholar]
- Beyer W., Imlay J., Fridovich I. Superoxide dismutases. Prog Nucleic Acid Res Mol Biol. 1991;40:221–253. doi: 10.1016/s0079-6603(08)60843-0. [DOI] [PubMed] [Google Scholar]
- Carlioz A., Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 1986 Mar;5(3):623–630. doi: 10.1002/j.1460-2075.1986.tb04256.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Close T. J., Rodriguez R. L. Construction and characterization of the chloramphenicol-resistance gene cartridge: a new approach to the transcriptional mapping of extrachromosomal elements. Gene. 1982 Dec;20(2):305–316. doi: 10.1016/0378-1119(82)90048-8. [DOI] [PubMed] [Google Scholar]
- Dowling J. N., Saha A. K., Glew R. H. Virulence factors of the family Legionellaceae. Microbiol Rev. 1992 Mar;56(1):32–60. doi: 10.1128/mr.56.1.32-60.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ely B. Genetics of Caulobacter crescentus. Methods Enzymol. 1991;204:372–384. doi: 10.1016/0076-6879(91)04019-k. [DOI] [PubMed] [Google Scholar]
- Farr S. B., D'Ari R., Touati D. Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8268–8272. doi: 10.1073/pnas.83.21.8268. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Farr S. B., Touati D., Kogoma T. Effects of oxygen stress on membrane functions in Escherichia coli: role of HPI catalase. J Bacteriol. 1988 Apr;170(4):1837–1842. doi: 10.1128/jb.170.4.1837-1842.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fridovich I. Superoxide radical: an endogenous toxicant. Annu Rev Pharmacol Toxicol. 1983;23:239–257. doi: 10.1146/annurev.pa.23.040183.001323. [DOI] [PubMed] [Google Scholar]
- Hassan H. M. Exacerbation of superoxide radical formation by paraquat. Methods Enzymol. 1984;105:523–532. doi: 10.1016/s0076-6879(84)05072-2. [DOI] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J Biol Chem. 1979 Nov 10;254(21):10846–10852. [PubMed] [Google Scholar]
- Hassan H. M. Microbial superoxide dismutases. Adv Genet. 1989;26:65–97. doi: 10.1016/s0065-2660(08)60223-0. [DOI] [PubMed] [Google Scholar]
- Kroll J. S., Langford P. R., Loynds B. M. Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae. J Bacteriol. 1991 Dec;173(23):7449–7457. doi: 10.1128/jb.173.23.7449-7457.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Latimer E., Simmers J., Sriranganathan N., Roop R. M., 2nd, Schurig G. G., Boyle S. M. Brucella abortus deficient in copper/zinc superoxide dismutase is virulent in BALB/c mice. Microb Pathog. 1992 Feb;12(2):105–113. doi: 10.1016/0882-4010(92)90113-3. [DOI] [PubMed] [Google Scholar]
- Minnich S. A., Ohta N., Taylor N., Newton A. Role of the 25-, 27-, and 29-kilodalton flagellins in Caulobacter crescentus cell motility: method for construction of deletion and Tn5 insertion mutants by gene replacement. J Bacteriol. 1988 Sep;170(9):3953–3960. doi: 10.1128/jb.170.9.3953-3960.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Poindexter J. S. The caulobacters: ubiquitous unusual bacteria. Microbiol Rev. 1981 Mar;45(1):123–179. doi: 10.1128/mr.45.1.123-179.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Puget K., Michelson A. M. Isolation of a new copper-containing superoxide dismutase bacteriocuprein. Biochem Biophys Res Commun. 1974 Jun 4;58(3):830–838. doi: 10.1016/s0006-291x(74)80492-4. [DOI] [PubMed] [Google Scholar]
- Smith P. K., Krohn R. I., Hermanson G. T., Mallia A. K., Gartner F. H., Provenzano M. D., Fujimoto E. K., Goeke N. M., Olson B. J., Klenk D. C. Measurement of protein using bicinchoninic acid. Anal Biochem. 1985 Oct;150(1):76–85. doi: 10.1016/0003-2697(85)90442-7. [DOI] [PubMed] [Google Scholar]
- Sriranganathan N., Boyle S. M., Schurig G., Misra H. Superoxide dismutases of virulent and avirulent strains of Brucella abortus. Vet Microbiol. 1991 Feb 15;26(4):359–366. doi: 10.1016/0378-1135(91)90029-f. [DOI] [PubMed] [Google Scholar]
- Steinman H. M. Bacteriocuprein superoxide dismutase of Photobacterium leiognathi. Isolation and sequence of the gene and evidence for a precursor form. J Biol Chem. 1987 Feb 5;262(4):1882–1887. [PubMed] [Google Scholar]
- Steinman H. M. Bacteriocuprein superoxide dismutases in pseudomonads. J Bacteriol. 1985 Jun;162(3):1255–1260. doi: 10.1128/jb.162.3.1255-1260.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Steinman H. M. Copper-zinc superoxide dismutase from Caulobacter crescentus CB15. A novel bacteriocuprein form of the enzyme. J Biol Chem. 1982 Sep 10;257(17):10283–10293. [PubMed] [Google Scholar]
- Steinman H. M., Ely B. Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning, sequencing, and mapping of the gene and periplasmic location of the enzyme. J Bacteriol. 1990 Jun;172(6):2901–2910. doi: 10.1128/jb.172.6.2901-2910.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tatum F. M., Detilleux P. G., Sacks J. M., Halling S. M. Construction of Cu-Zn superoxide dismutase deletion mutants of Brucella abortus: analysis of survival in vitro in epithelial and phagocytic cells and in vivo in mice. Infect Immun. 1992 Jul;60(7):2863–2869. doi: 10.1128/iai.60.7.2863-2869.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Touati D. Molecular genetics of superoxide dismutases. Free Radic Biol Med. 1988;5(5-6):393–402. doi: 10.1016/0891-5849(88)90113-x. [DOI] [PubMed] [Google Scholar]
- Yu J., Shapiro L. Early Caulobacter crescentus genes fliL and fliM are required for flagellar gene expression and normal cell division. J Bacteriol. 1992 May;174(10):3327–3338. doi: 10.1128/jb.174.10.3327-3338.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zhang Q. M., Yonei S. Induction of manganese-superoxide dismutase by membrane-binding drugs in Escherichia coli. J Bacteriol. 1991 Jun;173(11):3488–3491. doi: 10.1128/jb.173.11.3488-3491.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]


