Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1971 Dec;125(4):1075–1080. doi: 10.1042/bj1251075

Control of leghaemoglobin synthesis in snake beans

W J Broughton 1,*, M J Dilworth 1
PMCID: PMC1178271  PMID: 5144223

Abstract

1. The finding that the plant is the genetic determinant of leghaemoglobin production in legume nodules was further tested by inoculating snake beans with two strains of Rhizobium selected to give large genetic differences. Carbohydrate requirement patterns, immunological techniques and DNA base ratio determinations were used to demonstrate genetic differences between the two rhizobial strains. 2. Partially purified preparations of the haemoglobins from the nodules produced by the two strains showed no differences when examined by electrophoresis, isoelectric focusing or ion-exchange chromatography. 3. Two different leghaemoglobins from each type of nodule were separated by chromatography on DEAE-cellulose. One of these was isolated in the Fe3+ form and accounted for two-thirds of the total leghaemoglobin. When it was examined in the analytical ultracentrifuge and by amino acid analysis, this major component did not vary with the inoculant rhizobial strain. The molecule had an s20,w of 1.88S, a diffusion coefficient of 10.7×10−7cm2·s−1 and a mol. wt. of 16700. 4. These results strongly support the hypothesis that the mRNA for leghaemoglobin is transcribed from plant DNA.

Full text

PDF
1075

Images in this article

1078-1PLATE 1
on p.1078-1
1078-2PLATE 2
on p.1078-2

Selected References

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

  1. Appleby C. A. Properties of leghaemoglobin in vivo, and its isolation as ferrous oxyleghaemoglobin. Biochim Biophys Acta. 1969;188(2):222–229. doi: 10.1016/0005-2795(69)90069-5. [DOI] [PubMed] [Google Scholar]
  2. Appleby C. A. The separation and properties of low-spin (haemochrome) and native, high-spin forms of leghaemoglobin from soybean nodule extracts. Biochim Biophys Acta. 1969 Oct 21;189(2):267–279. doi: 10.1016/0005-2728(69)90053-x. [DOI] [PubMed] [Google Scholar]
  3. BOARDMAN N. K., ADAIR G. S. Isolation of two myoglobins from horseheart extracts and the determination of the molecular weight of the main component. Nature. 1956 Jun 9;177(4519):1078–1079. doi: 10.1038/1771078a0. [DOI] [PubMed] [Google Scholar]
  4. Catsimpoolas N. Micro isoelectric focusing in polyacrylamide gel columns. Anal Biochem. 1968 Dec;26(3):480–482. doi: 10.1016/0003-2697(68)90219-4. [DOI] [PubMed] [Google Scholar]
  5. Cutting J. A., Schulman H. M. The biogenesis of leghemoglobin. The determinant in the Rhizobium-legume symbiosis for leghemoglobin specificity. Biochim Biophys Acta. 1971 Jan 19;229(1):58–62. [PubMed] [Google Scholar]
  6. De Ley J., Rassel A. DNA base composition, flagellation and taxonomy of the genus Rhizobium. J Gen Microbiol. 1965 Oct;41(1):85–91. doi: 10.1099/00221287-41-1-85. [DOI] [PubMed] [Google Scholar]
  7. Dilworth M. J. The plant as the genetic determinant of leghaemoglobin production in the legume root nodule. Biochim Biophys Acta. 1969 Jul 30;184(2):432–441. doi: 10.1016/0304-4165(69)90047-6. [DOI] [PubMed] [Google Scholar]
  8. GRAHAM P. H. STUDIES ON THE UTILISATION OF CARBOHYDRATES AND KREBS CYCLE INTERMEDIATES BY RHIZOBIA, USING AN AGAR PLATE METHOD. Antonie Van Leeuwenhoek. 1964;30:68–72. doi: 10.1007/BF02046703. [DOI] [PubMed] [Google Scholar]
  9. Vincent J. M., Humphrey B. Taxonomically significant group antigens in Rhizobium. J Gen Microbiol. 1970 Nov;63(3):379–382. doi: 10.1099/00221287-63-3-379. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES