Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1997 Apr;113(4):1081–1090. doi: 10.1104/pp.113.4.1081

Novel, highly expressed late nodulin gene (LjNOD16) from Lotus japonicus.

P Kapranov 1, F J de Bruijn 1, K Szczyglowski 1
PMCID: PMC158231  PMID: 9112769

Abstract

We have isolated a Lotus japonicus cDNA corresponding to a highly abundant, late nodule-specific RNA species that encodes a polypeptide with a predicted molecular mass of 15.6 kD. The protein and its corresponding gene were designated Nlj16 and LjNOD16, respectively. LjNOD16 was found to be expressed only in the infected cells of L. japonicus nodules. Related DNA sequences could be identified in the genomes of both Glycine max and Medicago sativa. In the latter, a homologous mRNA species was detected in the nodules. Unlike LjNOD16, its alfalfa homologs appear to represent low-abundance mRNA species. However, the proteins corresponding to the LjNOD16 and its alfalfa homolog could be detected at similar levels in nodules but not in roots of both legume species. The predicted amino acid sequence analysis of nodulin Nlj16 revealed the presence of a long alpha-helical region and a positively charged C terminus. The former domain has a very high propensity to form a coiled-coil type structure, indicating that nodulin Nlj16 may interact with an as-yet-unidentified protein target(s) in the nodule-infected cells. Homology searches revealed no significant similarities to any known sequences in the databases, with the exception of two related, anonymous Arabidopsis expressed sequence tags.

Full Text

The Full Text of this article is available as a PDF (3.9 MB).

Selected References

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

  1. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  2. Bergmann H., Preddie E., Verma D. P. Nodulin-35: a subunit of specific uricase (uricase II) induced and localized in the uninfected cells of soybean nodules. EMBO J. 1983;2(12):2333–2339. doi: 10.1002/j.1460-2075.1983.tb01743.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boroń L. J., Legocki A. B. Cloning and characterization of a nodule-enhanced glutamine synthetase-encoding gene from Lupinus luteus. Gene. 1993 Dec 22;136(1-2):95–102. doi: 10.1016/0378-1119(93)90452-9. [DOI] [PubMed] [Google Scholar]
  4. Boroń L., Szczygłowski K., Konieczny A., Legocki A. B. Glutamine synthetase in Lupinus luteus. Identification and preliminary characterization of nodule-specific cDNA clone. Acta Biochim Pol. 1989;36(3-4):295–301. [PubMed] [Google Scholar]
  5. Brisson N., Pombo-Gentile A., Verma D. P. Organization and expression of leghaemoglobin genes. Can J Biochem. 1982 Mar;60(3):272–278. doi: 10.1139/o82-032. [DOI] [PubMed] [Google Scholar]
  6. Broughton W. J., Dilworth M. J. Control of leghaemoglobin synthesis in snake beans. Biochem J. 1971 Dec;125(4):1075–1080. doi: 10.1042/bj1251075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Church G. M., Gilbert W. Genomic sequencing. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1991–1995. doi: 10.1073/pnas.81.7.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Cook D., Dreyer D., Bonnet D., Howell M., Nony E., VandenBosch K. Transient induction of a peroxidase gene in Medicago truncatula precedes infection by Rhizobium meliloti. Plant Cell. 1995 Jan;7(1):43–55. doi: 10.1105/tpc.7.1.43. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Csanádi G., Szécsi J., Kaló P., Kiss P., Endre G., Kondorosi A., Kondorosi E., Kiss G. B. ENOD12, an early nodulin gene, is not required for nodule formation and efficient nitrogen fixation in alfalfa. Plant Cell. 1994 Feb;6(2):201–213. doi: 10.1105/tpc.6.2.201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fortin M. G., Morrison N. A., Verma D. P. Nodulin-26, a peribacteroid membrane nodulin is expressed independently of the development of the peribacteroid compartment. Nucleic Acids Res. 1987 Jan 26;15(2):813–824. doi: 10.1093/nar/15.2.813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fortin M. G., Zelechowska M., Verma D. P. Specific targeting of membrane nodulins to the bacteroid-enclosing compartment in soybean nodules. EMBO J. 1985 Dec 1;4(12):3041–3046. doi: 10.1002/j.1460-2075.1985.tb04043.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gebhardt C., Oliver J. E., Forde B. G., Saarelainen R., Miflin B. J. Primary structure and differential expression of glutamine synthetase genes in nodules, roots and leaves of Phaseolus vulgaris. EMBO J. 1986 Jul;5(7):1429–1435. doi: 10.1002/j.1460-2075.1986.tb04379.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hall T. C., Ma Y., Buchbinder B. U., Pyne J. W., Sun S. M., Bliss F. A. Messenger RNA for G1 protein of French bean seeds: Cell-free translation and product characterization. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3196–3200. doi: 10.1073/pnas.75.7.3196. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Heard J., Dunn K. Symbiotic induction of a MADS-box gene during development of alfalfa root nodules. Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5273–5277. doi: 10.1073/pnas.92.12.5273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  16. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  17. Legocki R. P., Verma D. P. A nodule-specific plant protein (nodulin-35) from soybean. Science. 1979 Jul 13;205(4402):190–193. doi: 10.1126/science.205.4402.190. [DOI] [PubMed] [Google Scholar]
  18. Lerouge P., Roche P., Faucher C., Maillet F., Truchet G., Promé J. C., Dénarié J. Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signal. Nature. 1990 Apr 19;344(6268):781–784. doi: 10.1038/344781a0. [DOI] [PubMed] [Google Scholar]
  19. Liang P., Pardee A. B. Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science. 1992 Aug 14;257(5072):967–971. doi: 10.1126/science.1354393. [DOI] [PubMed] [Google Scholar]
  20. Lupas A. Prediction and analysis of coiled-coil structures. Methods Enzymol. 1996;266:513–525. doi: 10.1016/s0076-6879(96)66032-7. [DOI] [PubMed] [Google Scholar]
  21. Miao G. H., Verma D. P. Soybean nodulin-26 gene encoding a channel protein is expressed only in the infected cells of nodules and is regulated differently in roots of homologous and heterologous plants. Plant Cell. 1993 Jul;5(7):781–794. doi: 10.1105/tpc.5.7.781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Mylona P., Pawlowski K., Bisseling T. Symbiotic Nitrogen Fixation. Plant Cell. 1995 Jul;7(7):869–885. doi: 10.1105/tpc.7.7.869. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 1994 May;19(1):55–72. doi: 10.1002/prot.340190108. [DOI] [PubMed] [Google Scholar]
  24. Rost B., Sander C. Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol. 1993 Jul 20;232(2):584–599. doi: 10.1006/jmbi.1993.1413. [DOI] [PubMed] [Google Scholar]
  25. Spaink H. P. Rhizobial lipo-oligosaccharides: answers and questions. Plant Mol Biol. 1992 Dec;20(5):977–986. doi: 10.1007/BF00027167. [DOI] [PubMed] [Google Scholar]
  26. Thummler F., Verma D. P. Nodulin-100 of soybean is the subunit of sucrose synthase regulated by the availability of free heme in nodules. J Biol Chem. 1987 Oct 25;262(30):14730–14736. [PubMed] [Google Scholar]
  27. 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]
  28. Verma DPS. Signals in Root Nodule Organogenesis and Endocytosis of Rhizobium. Plant Cell. 1992 Apr;4(4):373–382. doi: 10.1105/tpc.4.4.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Verwoerd T. C., Dekker B. M., Hoekema A. A small-scale procedure for the rapid isolation of plant RNAs. Nucleic Acids Res. 1989 Mar 25;17(6):2362–2362. doi: 10.1093/nar/17.6.2362. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Welsh J., Chada K., Dalal S. S., Cheng R., Ralph D., McClelland M. Arbitrarily primed PCR fingerprinting of RNA. Nucleic Acids Res. 1992 Oct 11;20(19):4965–4970. doi: 10.1093/nar/20.19.4965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. van de Wiel C., Scheres B., Franssen H., van Lierop M. J., van Lammeren A., van Kammen A., Bisseling T. The early nodulin transcript ENOD2 is located in the nodule parenchyma (inner cortex) of pea and soybean root nodules. EMBO J. 1990 Jan;9(1):1–7. doi: 10.1002/j.1460-2075.1990.tb08073.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES