Abstract
LEGHAEMOGLOBIN (Lb), a myoglobin-like protein, is found in large quantities in the root nodules which result from the symbiotic association between the bacterium Rhizobium and plants of the family Leguminosae. The probable function of Lb is the regulation of intranodule oxygen tension1 and its presence is correlated with rhizobial nitrogenase2. The haem prosthetic group of Lb is of bacterial origin3 and the plant contains the genetic determinants for the apoprotein4,5. Soybean Lb consists of two major components of different electrophoretic mobility6. The faster component (LbF) is composed of 139 amino acids, has a molecular weight of 15,600 and contains an amino terminal glycine residue, while the slower component (LbS) is composed of 143 amino acids, has a molecular weight of 15,900 and contains an amino terminal valine residue. Because of these differences LbF and LbS are presumed to be different gene products7. Thus they are useful markers in studies on the transfer of plant genes involved in symbiosis to other plants.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Bergersen, F. J., Turner, G. L., and Appleby, C. A., Biochim. biophys. Acta, 292, 271–282 (1973).
Virtanen, A. I., Jorma, J., Linkola, H., and Linnasalmi, A., Acta chem. Scand., 1, 90–111 (1947).
Cutting, J. A., and Schulman, H. M., Biochim. biophys. Acta, 192, 486–493 (1969).
Dilworth, M. J., Biochim. biophys. Acta, 184, 432–441 (1969).
Cutting, J. A., and Schulman, H. M., Biochim. biophys. Acta, 229, 58–62 (1971).
Ellfolk, N., Acta chem. Scand., 15, 545–554 (1961).
Broughton, W. J., and Dilworth, M. J., Biochim. biophys. Acta, 317, 266–276 (1973).
Palmiter, R. D., Oka, T., and Schimke, R. T., J. biol. Chem., 246, 724–737 (1971).
Seal, S. N., Bewley, J. D., and Marcus, A., J. biol. Chem., 247, 2592–2597 (1972).
Weeks, D. P., Verma, D. P. S., Seal, S. N., and Marcus, A., Nature, 236, 167–168 (1972).
Weeks, D. P., and Marcus, A., Biochim. biophys. Acta, 232, 671–684 (1971).
Aviv, H., and Leder, P., Proc. natn. Acad. Sci. U.S.A., 69, 1408–1412 (1972).
Loening, U. E., Biochem. J., 113, 131–138 (1969).
Davis, B. J., Ann. N. Y. Acad. Sci., 121, 404–427 (1964).
Bunn, H. F., and Jandl, J. H., J. biol. Chem., 243, 465–475 (1968).
Efron, D., and Marcus, A., FEBS Lett., 33, 23–27 (1973).
Burr, H., and Lingrel, J. B., Nature new Biol., 233, 41–43 (1971).
Van de Walle, C., FEBS Lett., 34, 31–34 (1973).
Molloy, G. R., Sporn, M. B., Kelley, D. E., and Perry, R. P., Biochemistry, 11, 3256–3260 (1972).
Nakazato, H., Kopp, D. W., and Edmonds, M., J. biol. Chem., 248, 1472–1476 (1972).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
VERMA, D., NASH, D. & SCHULMAN, H. Isolation and in vitro translation of soybean leghaemoglobin mRNA. Nature 251, 74–77 (1974). https://doi.org/10.1038/251074a0
Received:
Revised:
Issue date:
DOI: https://doi.org/10.1038/251074a0
This article is cited by
-
Immunogold localization of glutamine synthetase in soybean leaves, roots, and nodules
Protoplasma (1989)
-
A block in the endocytosis of Rhizobium allows cellular differentiation in nodules but affects the expression of some peribacteroid membrane nodulins
Plant Molecular Biology (1987)
-
Expression of host genes during root nodule development in soybeans
Molecular and General Genetics MGG (1986)
-
Expression of nodule-specific glutamine synthetase genes during nodule development in soybeans
Plant Molecular Biology (1986)
