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. 1985 Apr;162(1):430–433. doi: 10.1128/jb.162.1.430-433.1985

Dimeric porin from Paracoccus denitrificans.

L S Zalman, H Nikaido
PMCID: PMC219007  PMID: 2984184

Abstract

Paracoccus denitrificans was shown to contain a 33,000-dalton porin, which produced pores of large (1.6 to 1.8 nm) diameter. Cross-linking studies showed that the porin existed as dimers in the outer membrane.

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Selected References

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  1. Angus B. L., Hancock R. E. Outer membrane porin proteins F, P, and D1 of Pseudomonas aeruginosa and PhoE of Escherichia coli: chemical cross-linking to reveal native oligomers. J Bacteriol. 1983 Sep;155(3):1042–1051. doi: 10.1128/jb.155.3.1042-1051.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Banker G. A., Cotman C. W. Measurement of free electrophoretic mobility and retardation coefficient of protein-sodium dodecyl sulfate complexes by gel electrophoresis. A method to validate molecular weight estimates. J Biol Chem. 1972 Sep 25;247(18):5856–5861. [PubMed] [Google Scholar]
  3. Benz R., Hancock R. E. Properties of the large ion-permeable pores formed from protein F of Pseudomonas aeruginosa in lipid bilayer membranes. Biochim Biophys Acta. 1981 Aug 20;646(2):298–308. doi: 10.1016/0005-2736(81)90336-9. [DOI] [PubMed] [Google Scholar]
  4. Davies G. E., Stark G. R. Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. Proc Natl Acad Sci U S A. 1970 Jul;66(3):651–656. doi: 10.1073/pnas.66.3.651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Flammann H. T., Weckesser J. Porin isolated from the cell envelope of Rhodopseudomonas capsulata. J Bacteriol. 1984 Jul;159(1):410–412. doi: 10.1128/jb.159.1.410-412.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fox G. E., Stackebrandt E., Hespell R. B., Gibson J., Maniloff J., Dyer T. A., Wolfe R. S., Balch W. E., Tanner R. S., Magrum L. J. The phylogeny of prokaryotes. Science. 1980 Jul 25;209(4455):457–463. doi: 10.1126/science.6771870. [DOI] [PubMed] [Google Scholar]
  7. Hancock R. E., Decad G. M., Nikaido H. Identification of the protein producing transmembrane diffusion pores in the outer membrane of Pseudomonas aeruginosa PA01. Biochim Biophys Acta. 1979 Jul 5;554(2):323–331. doi: 10.1016/0005-2736(79)90373-0. [DOI] [PubMed] [Google Scholar]
  8. Hancock R. E., Poole K., Benz R. Outer membrane protein P of Pseudomonas aeruginosa: regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes. J Bacteriol. 1982 May;150(2):730–738. doi: 10.1128/jb.150.2.730-738.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lomant A. J., Fairbanks G. Chemical probes of extended biological structures: synthesis and properties of the cleavable protein cross-linking reagent [35S]dithiobis(succinimidyl propionate). J Mol Biol. 1976 Jun 14;104(1):243–261. doi: 10.1016/0022-2836(76)90011-5. [DOI] [PubMed] [Google Scholar]
  10. Luckey M., Nikaido H. Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Jan;77(1):167–171. doi: 10.1073/pnas.77.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mannella C. A., Colombini M., Frank J. Structural and functional evidence for multiple channel complexes in the outer membrane of Neurospora crassa mitochondria. Proc Natl Acad Sci U S A. 1983 Apr;80(8):2243–2247. doi: 10.1073/pnas.80.8.2243. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Nakae T., Ishii J., Tokunaga M. Subunit structure of functional porin oligomers that form permeability channels in the other membrane of Escherichia coli. J Biol Chem. 1979 Mar 10;254(5):1457–1461. [PubMed] [Google Scholar]
  13. Nakamura K., Mizushima S. Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12. J Biochem. 1976 Dec;80(6):1411–1422. doi: 10.1093/oxfordjournals.jbchem.a131414. [DOI] [PubMed] [Google Scholar]
  14. Nikaido H., Nakae T. The outer membrane of Gram-negative bacteria. Adv Microb Physiol. 1979;20:163–250. doi: 10.1016/s0065-2911(08)60208-8. [DOI] [PubMed] [Google Scholar]
  15. Nikaido H. Proteins forming large channels from bacterial and mitochondrial outer membranes: porins and phage lambda receptor protein. Methods Enzymol. 1983;97:85–100. doi: 10.1016/0076-6879(83)97122-7. [DOI] [PubMed] [Google Scholar]
  16. Palva E. T., Randall L. L. Arrangement of protein I in Escherichia coli outer membrane: cross-linking study. J Bacteriol. 1978 Jan;133(1):279–286. doi: 10.1128/jb.133.1.279-286.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Palva E. T., Westermann P. Arrangement of the maltose-inducible major outer membrane proteins, the bacteriophage lambda receptor in Escherichia coli and the 44 K protein in Salmonella typhimurium. FEBS Lett. 1979 Mar 1;99(1):77–80. doi: 10.1016/0014-5793(79)80253-7. [DOI] [PubMed] [Google Scholar]
  18. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  19. Smit J., Kamio Y., Nikaido H. Outer membrane of Salmonella typhimurium: chemical analysis and freeze-fracture studies with lipopolysaccharide mutants. J Bacteriol. 1975 Nov;124(2):942–958. doi: 10.1128/jb.124.2.942-958.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Steven A. C., Heggeler B., Müller R., Kistler J., Rosenbusch J. P. Ultrastructure of a periodic protein layer in the outer membrane of Escherichia coli. J Cell Biol. 1977 Feb;72(2):292–301. doi: 10.1083/jcb.72.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Szmelcman S., Schwartz M., Silhavy T. J., Boos W. Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching. Eur J Biochem. 1976 May 17;65(1):13–19. doi: 10.1111/j.1432-1033.1976.tb10383.x. [DOI] [PubMed] [Google Scholar]
  22. Tokunaga M., Tokunaga H., Okajima Y., Nakae T. Characterization of porins from the outer membrane of Salmonella typhimurium. 2. Physical properties of the functional oligomeric aggregates. Eur J Biochem. 1979 Apr;95(3):441–448. doi: 10.1111/j.1432-1033.1979.tb12983.x. [DOI] [PubMed] [Google Scholar]
  23. Weckesser J., Zalman L. S., Nikaido H. Porin from Rhodopseudomonas sphaeroides. J Bacteriol. 1984 Jul;159(1):199–205. doi: 10.1128/jb.159.1.199-205.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Yoshimura F., Zalman L. S., Nikaido H. Purification and properties of Pseudomonas aeruginosa porin. J Biol Chem. 1983 Feb 25;258(4):2308–2314. [PubMed] [Google Scholar]

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