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. 1979 Apr;138(1):207–217. doi: 10.1128/jb.138.1.207-217.1979

Modifiable chromatophore proteins in photosynthetic bacteria.

K M Hui, R E Hurlbert
PMCID: PMC218259  PMID: 438130

Abstract

The chromatophores of Chromatium vinosum, as well as six other photosynthetic bacteria, contained two or more proteins which were insoluble when heated in the presence of sodium dodecyl sulfate (SDS) and 2-mercaptoethanol (beta-ME). When the chromatophores were dissolved at room temperature in SDS-beta-ME, these proteins were present in the SDS-polyacrylamide gel electrophoresis profiles, but when the samples were dissolved at 100 degrees C, they were absent or considerably diminished. When one-dimensional gels of chromatophores solubilized at room temperature were soaked in the SDS-beta-ME solution and heated to 100 degrees C and the gels were run in a second dimension, the proteins became immobilized in the original first-dimension gel, where they could be detected by staining. The two major proteins so affected in C. vinosum had apparent molecular weights of 28,000 and 21,000. The chromatophores of several other photosynthetic bacteria also contained predominant proteins between 30,000 and 19,000 molecular weight, which became insoluble when heated in the presence of SDS and beta-ME. In at least two of the species examined, these appeared to be reaction center proteins. The conditions causing the proteins to become insoluble were complex and involved temperature, SDS concentration, and the presence of sulfhydryl reagents. The chromatophores of four of the Chromatiaceae species and two strains of one of the Rhodospirillaceae species examined had a protein-pigment complex that was visible in SDS-polyacrylamide gel profiles of samples dissolved at room temperature but was absent in samples dissolved at 100 degrees C.

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Selected References

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

  1. COHEN-BAZIRE G., KUNISAWA R. The fine structure of Rhodospirillum rubrum. J Cell Biol. 1963 Feb;16:401–419. doi: 10.1083/jcb.16.2.401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Clayton R. K., Clayton B. J. Relations between pigments and proteins in the photosynthetic membranes of Rhodopseudomonas spheroides. Biochim Biophys Acta. 1972 Dec 14;283(3):492–504. doi: 10.1016/0005-2728(72)90265-4. [DOI] [PubMed] [Google Scholar]
  3. Clayton R. K., Haselkorn R. Protein components of bacterial photosynthetic membranes. J Mol Biol. 1972 Jul 14;68(1):97–105. doi: 10.1016/0022-2836(72)90265-3. [DOI] [PubMed] [Google Scholar]
  4. Cohen-Bazire G., Kunisawa R. SOME OBSERVATIONS ON THE SYNTHESIS AND FUNCTION OF THE PHOTOSYNTHETIC APPARATUS IN RHODOSPIRILLUM RUBRUM. Proc Natl Acad Sci U S A. 1960 Dec;46(12):1543–1553. doi: 10.1073/pnas.46.12.1543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Collins M. L., Niederman R. A. Membranes of Rhodospirillum rubrum: physicochemical properties of chromatophore fractions isolated from osmotically and mechanically disrupted cells. J Bacteriol. 1976 Jun;126(3):1326–1338. doi: 10.1128/jb.126.3.1326-1338.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Drews G., Dierstein R., Schumacher A. Genetic transfer of the capacity to form bacteriochlorophyll-protein complexes in Rhodopseudomonas capsulata. FEBS Lett. 1976 Sep 15;68(1):132–136. doi: 10.1016/0014-5793(76)80421-8. [DOI] [PubMed] [Google Scholar]
  7. Drews G., Witzemann V. Zur Taxonomie von Rhodopseudomonas palustris. Arch Mikrobiol. 1971;78(4):322–329. doi: 10.1007/BF00412272. [DOI] [PubMed] [Google Scholar]
  8. Fraker P. J., Kaplan S. Isolation and characterization of a bacteriochlorophyll-containing protein from Rhodopseudomonas spheroides. J Biol Chem. 1972 May 10;247(9):2732–2737. [PubMed] [Google Scholar]
  9. Fraker P. J., Kaplan S. Isolation and fractionation of the photosynthetic membranous organelles from Rhodopseudomonas spheroides. J Bacteriol. 1971 Oct;108(1):465–473. doi: 10.1128/jb.108.1.465-473.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Garcia A., Vernon L. P., Mollenhauer H. Properties of Chromatium subchromatophore particles obtained by treatment with Triton X-100. Biochemistry. 1966 Jul;5(7):2399–2407. doi: 10.1021/bi00871a033. [DOI] [PubMed] [Google Scholar]
  11. HOLT S. C., MARR A. G. ISOLATION AND PURIFICATION OF THE INTRACYTOPLASMIC MEMBRANES OF RHODOSPIRILLUM RUBRUM. J Bacteriol. 1965 May;89:1413–1420. doi: 10.1128/jb.89.5.1413-1420.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. HURLBERT R. E., LASCELLES J. RIBULOSE DIPHOSPHATE CARBOXYLASE IN THIORHODACEAE. J Gen Microbiol. 1963 Dec;33:445–458. doi: 10.1099/00221287-33-3-445. [DOI] [PubMed] [Google Scholar]
  13. Halsey Y. D., Gyers B. A large photoreactive particle from Chromatium vinosum chromatophores. Biochim Biophys Acta. 1975 May 15;387(2):349–367. doi: 10.1016/0005-2728(75)90115-2. [DOI] [PubMed] [Google Scholar]
  14. Huang J. W., Kaplan S. Membrane proteins of Rhodopseudomonas spheroides. 3. Isolation, purification, and characterization of cell envelope proteins. Biochim Biophys Acta. 1973 May 11;307(2):301–316. doi: 10.1016/0005-2736(73)90097-7. [DOI] [PubMed] [Google Scholar]
  15. Hurlbert R. E. Isolation and characterization of Chromatium vinosum membranes. Arch Microbiol. 1974;101(2):169–186. doi: 10.1007/BF00455937. [DOI] [PubMed] [Google Scholar]
  16. Ketchum P. A., Holt S. C. Isolation and characterization of the membranes from Rhodospirillum rubrum. Biochim Biophys Acta. 1970;196(2):141–161. doi: 10.1016/0005-2736(70)90002-7. [DOI] [PubMed] [Google Scholar]
  17. King J., Laemmli U. K. Polypeptides of the tail fibres of bacteriophage T4. J Mol Biol. 1971 Dec 28;62(3):465–477. doi: 10.1016/0022-2836(71)90148-3. [DOI] [PubMed] [Google Scholar]
  18. King M. T., Drews G. The function and localization of ubiquinone in the NADH and succinate oxidase systems of Rhodopseudomonas palustris. Biochim Biophys Acta. 1973 May 30;305(2):230–248. doi: 10.1016/0005-2728(73)90172-2. [DOI] [PubMed] [Google Scholar]
  19. Lien S., Gest H., San Pietro A. Regulation of chlorophyll synthesis in photosynthetic bacteria. J Bioenerg. 1973;4(4):423–434. doi: 10.1007/BF01648969. [DOI] [PubMed] [Google Scholar]
  20. Niederman R. A., Segen B. J., Gibson K. D. Membranes of Rhodopseudomonas spheroides. I. Isolation and characterization of membrane fractions from extracts of aerobically and anaerobically grown cells. Arch Biochem Biophys. 1972 Oct;152(2):547–560. doi: 10.1016/0003-9861(72)90250-0. [DOI] [PubMed] [Google Scholar]
  21. Nieth K. F., Drews G., Feick R. Photochemical reaction centers from Rhodopseudomonas capsulata. Arch Microbiol. 1975 Sep 30;105(1):43–45. doi: 10.1007/BF00447110. [DOI] [PubMed] [Google Scholar]
  22. Nieth K. F., Drews G. Formation of reaction centers and light-harvesting bacteriochlorophyll-protein complexes in Rhodopseudomonas capsulata. Arch Microbiol. 1975 Jun 20;104(1):77–82. doi: 10.1007/BF00447303. [DOI] [PubMed] [Google Scholar]
  23. Nieth K. F., Drews G. The protein patterns of intracytoplasmic membranes and reaction center particles isolated from Rhodopseudomonas capsulata. Arch Mikrobiol. 1974 Mar 4;96(2):161–174. doi: 10.1007/BF00590173. [DOI] [PubMed] [Google Scholar]
  24. Noël H., Van der Rest M., Gingras G. Isolation and partial characterization of P870 reaction center complex from wild type Rhodospirillum rubrum. Biochim Biophys Acta. 1972 Aug 17;275(2):219–230. doi: 10.1016/0005-2728(72)90043-6. [DOI] [PubMed] [Google Scholar]
  25. Oelze J., Drews G. Membranes of photosynthetic bacteria. Biochim Biophys Acta. 1972 Apr 18;265(2):209–239. doi: 10.1016/0304-4157(72)90003-2. [DOI] [PubMed] [Google Scholar]
  26. Okamura M. Y., Steiner L. A., Feher G. Characterization of reaction centers from photosynthetic bacteria. I. Subunit structure of the protein mediating the primary photochemistry in Rhodopseudomonas spheroides R-26. Biochemistry. 1974 Mar 26;13(7):1394–1403. doi: 10.1021/bi00704a013. [DOI] [PubMed] [Google Scholar]
  27. Prince R. C., Crofts A. R. Photochemical reaction centres from Rhodopseudomonas capsulata Ala pho+. FEBS Lett. 1973 Sep 15;35(2):213–216. doi: 10.1016/0014-5793(73)80287-x. [DOI] [PubMed] [Google Scholar]
  28. Reed D. W., Raveed D., Israel H. W. Functional bacteriochlorophyll-protein complexes from chromatophores of Rhodopseudomonas spheroides strain R-26. Biochim Biophys Acta. 1970 Dec 8;223(2):281–291. doi: 10.1016/0005-2728(70)90185-4. [DOI] [PubMed] [Google Scholar]
  29. Reithmeier R. A., Bragg P. D. Molecular characterization of a heat-modifiable protein from the outer membrane of Escherichia coli. Arch Biochem Biophys. 1977 Jan 30;178(2):527–534. doi: 10.1016/0003-9861(77)90223-5. [DOI] [PubMed] [Google Scholar]
  30. Russell R. R. Two-dimensional SDS-polyacrylamide gel electrophoresis of heat-modifiable outer-membrane proteins. Can J Microbiol. 1976 Jan;22(1):83–91. doi: 10.1139/m76-011. [DOI] [PubMed] [Google Scholar]
  31. Schnaitman C. A. Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J Bacteriol. 1971 Oct;108(1):545–552. doi: 10.1128/jb.108.1.545-552.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Scurzi W., Fishbein W. N. The geometric mobility sequence in polyacrylamide gel electrophoresis of polymeric proteins: its significance for polymer geometry and electrophoretic theory. Trans N Y Acad Sci. 1973 May;35(5):396–416. doi: 10.1111/j.2164-0947.1973.tb01979.x. [DOI] [PubMed] [Google Scholar]
  33. Shepherd W. D., Kaplan S. Effect of heat and 2-mercaptoethanol on intracytoplasmic membrane polypeptides of Rhodopseudomonas sphaeroides. J Bacteriol. 1978 Aug;135(2):656–667. doi: 10.1128/jb.135.2.656-667.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Steiner L. A., Okamura M. Y., Lopes A. D., Moskowitz E., Feher G. Characterization of reaction centers from photosynthetic bacteria. II. Amino acid composition of the reaction center protein and its subunits in Rhodopseudomonas spheroides R-26. Biochemistry. 1974 Mar 26;13(7):1403–1410. doi: 10.1021/bi00704a014. [DOI] [PubMed] [Google Scholar]
  35. Takemoto J., Lascelles J. Function of membrane proteins coupled to bacteriochlorophyll synthesis. Studies with wild type and mutant strains of Rhodopseudomonas spheroides. Arch Biochem Biophys. 1974 Aug;163(2):507–514. doi: 10.1016/0003-9861(74)90508-6. [DOI] [PubMed] [Google Scholar]
  36. Tonn S. J., Gogel G. E., Loach P. A. Isolation and characterization of an organic solvent soluble polypeptide component from photoreceptor complexes of Rhodospirillum rubrum. Biochemistry. 1977 Mar 8;16(5):877–885. doi: 10.1021/bi00624a011. [DOI] [PubMed] [Google Scholar]
  37. WORDEN P. B., SISTROM W. R. THE PREPARATION AND PROPERTIES OF BACTERIAL CHROMATOPHORE FRACTIONS. J Cell Biol. 1964 Oct;23:135–150. doi: 10.1083/jcb.23.1.135. [DOI] [PMC free article] [PubMed] [Google Scholar]

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