Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1985 Jun;162(3):1255–1260. doi: 10.1128/jb.162.3.1255-1260.1985

Bacteriocuprein superoxide dismutases in pseudomonads.

H M Steinman
PMCID: PMC215912  PMID: 3997777

Abstract

Two new instances of the rare bacteriocuprein form of superoxide dismutase have been discovered in Pseudomonas diminuta and P. maltophilia. Each species contains a manganese superoxide dismutase as well. Eight other strains of Pseudomonas and Xanthomonas spp. lacked bacteriocupreins and contained either a manganese or an iron superoxide dismutase. Native molecular weights and isoelectric points were determined for all these bacterial dismutases. A monospecific polyclonal antibody was prepared against the bacteriocuprein from Photobacterium leiognathi; it was not cross-reactive with the bacteriocuprein from either Pseudomonas strain. Bacteriocupreins have previously been identified in only two procaryotes, P. leiognathi and Caulobacter crescentus. The discovery of the Pseudomonas bacteriocupreins reveals a broader distribution, raising the possibility that bacteriocupreins are a continuous line of descent among procaryotes and not isolated evolutionary occurrences, as previous data suggested.

Full text

PDF
1255

Images in this article

1257Image
on p.1257

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Batteiger B., Newhall W. J., 5th, Jones R. B. The use of Tween 20 as a blocking agent in the immunological detection of proteins transferred to nitrocellulose membranes. J Immunol Methods. 1982 Dec 30;55(3):297–307. doi: 10.1016/0022-1759(82)90089-8. [DOI] [PubMed] [Google Scholar]
  2. Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
  3. Blake M. S., Johnston K. H., Russell-Jones G. J., Gotschlich E. C. A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal Biochem. 1984 Jan;136(1):175–179. doi: 10.1016/0003-2697(84)90320-8. [DOI] [PubMed] [Google Scholar]
  4. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  5. Crapo J. D., McCord J. M., Fridovich I. Preparation and assay of superoxide dismutases. Methods Enzymol. 1978;53:382–393. doi: 10.1016/s0076-6879(78)53044-9. [DOI] [PubMed] [Google Scholar]
  6. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  7. Dovrat A., Gershon D. Studies on the fate of aldolase molecules in the aging rat lens. Biochim Biophys Acta. 1983 May 25;757(2):164–167. doi: 10.1016/0304-4165(83)90104-6. [DOI] [PubMed] [Google Scholar]
  8. Geller B. L., Winge D. R. A method for distinguishing Cu,Zn- and Mn-containing superoxide dismutases. Anal Biochem. 1983 Jan;128(1):86–92. doi: 10.1016/0003-2697(83)90348-2. [DOI] [PubMed] [Google Scholar]
  9. Gregory E. M., Fridovich I. Visualization of catalase on acrylamide gels. Anal Biochem. 1974 Mar;58(1):57–62. doi: 10.1016/0003-2697(74)90440-0. [DOI] [PubMed] [Google Scholar]
  10. Hawkes R., Niday E., Gordon J. A dot-immunobinding assay for monoclonal and other antibodies. Anal Biochem. 1982 Jan 1;119(1):142–147. doi: 10.1016/0003-2697(82)90677-7. [DOI] [PubMed] [Google Scholar]
  11. Hedrick J. L., Smith A. J. Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Arch Biochem Biophys. 1968 Jul;126(1):155–164. doi: 10.1016/0003-9861(68)90569-9. [DOI] [PubMed] [Google Scholar]
  12. Kanematsu S., Asada K. Ferric and manganic superoxide dismutases in Euglena gracilis. Arch Biochem Biophys. 1979 Jul;195(2):535–545. doi: 10.1016/0003-9861(79)90380-1. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Lönnerdal B., Keen C. L., Hurley L. S. Isoelectric focusing of superoxide dismutase isoenzymes. FEBS Lett. 1979 Dec 1;108(1):51–55. doi: 10.1016/0014-5793(79)81177-1. [DOI] [PubMed] [Google Scholar]
  15. Martin J. P., Jr, Fridovich I. Evidence for a natural gene transfer from the ponyfish to its bioluminescent bacterial symbiont Photobacter leiognathi. The close relationship between bacteriocuprein and the copper-zinc superoxide dismutase of teleost fishes. J Biol Chem. 1981 Jun 25;256(12):6080–6089. [PubMed] [Google Scholar]
  16. McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
  17. Nettleton C. J., Bull C., Baldwin T. O., Fee J. A. Isolation of the Escherichia coli iron superoxide dismutase gene: evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4970–4973. doi: 10.1073/pnas.81.15.4970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. OUCHTERLONY O. Diffusion-in-gel methods for immunological analysis. Prog Allergy. 1958;5:1–78. [PubMed] [Google Scholar]
  19. Puget K., Michelson A. M. Iron containing superoxide dismutases from luminous bacteria. Biochimie. 1974;56(9):1255–1267. doi: 10.1016/s0300-9084(74)80019-2. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. Sakamoto H., Touati D. Cloning of the iron superoxide dismutase gene (sodB) in Escherichia coli K-12. J Bacteriol. 1984 Jul;159(1):418–420. doi: 10.1128/jb.159.1.418-420.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Salin M. L., McCord J. M. Superoxide dismutases in polymorphonuclear leukocytes. J Clin Invest. 1974 Oct;54(4):1005–1009. doi: 10.1172/JCI107816. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sherman L., Dafni N., Lieman-Hurwitz J., Groner Y. Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA. Proc Natl Acad Sci U S A. 1983 Sep;80(18):5465–5469. doi: 10.1073/pnas.80.18.5465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Steffens G. J., Bannister J. V., Bannister W. H., Flohé L., Günzler W. A., Kim S. M., Otting F. The primary structure of Cu-Zn superoxide dismutase from Photobacterium leiognathi: evidence for a separate evolution of Cu-Zn superoxide dismutase in bacteria. Hoppe Seylers Z Physiol Chem. 1983 Jun;364(6):675–690. doi: 10.1515/bchm2.1983.364.1.675. [DOI] [PubMed] [Google Scholar]
  25. 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]
  26. Steinman H. M., Naik V. R., Abernethy J. L., Hill R. L. Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. J Biol Chem. 1974 Nov 25;249(22):7326–7338. [PubMed] [Google Scholar]
  27. Terech A., Vignais P. M. A manganese-containing superoxide dismutase from Paracoccus denitrificans. Biochim Biophys Acta. 1981 Feb 13;657(2):411–424. doi: 10.1016/0005-2744(81)90327-2. [DOI] [PubMed] [Google Scholar]
  28. Touati D. Cloning and mapping of the manganese superoxide dismutase gene (sodA) of Escherichia coli K-12. J Bacteriol. 1983 Sep;155(3):1078–1087. doi: 10.1128/jb.155.3.1078-1087.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Vignais P. M., Terech A., Meyer C. M., Henry M. F. Isolation and characterization of a protein with cyanide-sensitive superoxide dismutase activity from the prokaryote, Paracoccus denitrificans. Biochim Biophys Acta. 1982 Mar 4;701(3):305–317. doi: 10.1016/0167-4838(82)90233-3. [DOI] [PubMed] [Google Scholar]
  31. Weisiger R. A., Fridovich I. Superoxide dismutase. Organelle specificity. J Biol Chem. 1973 May 25;248(10):3582–3592. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES