Skip to main content
PMC home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1987 Jan 26;15(2):813–824. doi: 10.1093/nar/15.2.813

Nodulin-26, a peribacteroid membrane nodulin is expressed independently of the development of the peribacteroid compartment.

M G Fortin, N A Morrison, D P Verma
PMCID: PMC340469  PMID: 3822816

Abstract

The peribacteroid membrane (pbm) of root nodules is derived from the plant cell plasma membrane but contains in addition several nodule-specific host proteins (nodulins). Antibodies raised against purified pbm of soybean were used to immunoprecipitate polysomes to isolate an RNA fraction that served as a template for the synthesis of a cDNA probe for screening a nodule-specific cDNA library. Clone p1B1 was found to encode a 26.5 kDa polypeptide (nodulin-26) which is immunoprecipitable specifically with the anti-pbm serum. Nodulin-26 has features of a transmembrane protein and its structure differs from that of nodulin-24 which appears to be a surface protein of pbm. The expression of these two pbm nodulins was examined in nodules induced by Bradyrhizobium japonicum Tn5 mutants that arrest nodule development at different stages of pbm biosynthesis. Nodules that do not show release of bacteria from the infection thread express nodulin-24 at a very low level. In contrast, the expression of nodulin-26 occurs fully in nodules that form infection threads only and is not affected by the release of bacteria from the threads.

Full text

PDF
813

Images in this article

816Image
on p.816

Selected References

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

  1. Argos P., Narayana S. V., Nielsen N. C. Structural similarity between legumin and vicilin storage proteins from legumes. EMBO J. 1985 May;4(5):1111–1117. doi: 10.1002/j.1460-2075.1985.tb03747.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Eisenberg D. Three-dimensional structure of membrane and surface proteins. Annu Rev Biochem. 1984;53:595–623. doi: 10.1146/annurev.bi.53.070184.003115. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Fuller F., Künstner P. W., Nguyen T., Verma D. P. Soybean nodulin genes: Analysis of cDNA clones reveals several major tissue-specific sequences in nitrogen-fixing root nodules. Proc Natl Acad Sci U S A. 1983 May;80(9):2594–2598. doi: 10.1073/pnas.80.9.2594. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Katinakis P., Verma D. P. Nodulin-24 gene of soybean codes for a peptide of the peribacteroid membrane and was generated by tandem duplication of a sequence resembling an insertion element. Proc Natl Acad Sci U S A. 1985 Jun;82(12):4157–4161. doi: 10.1073/pnas.82.12.4157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Korman A. J., Knudsen P. J., Kaufman J. F., Strominger J. L. cDNA clones for the heavy chain of HLA-DR antigens obtained after immunopurification of polysomes by monoclonal antibody. Proc Natl Acad Sci U S A. 1982 Mar;79(6):1844–1848. doi: 10.1073/pnas.79.6.1844. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kozak M. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev. 1983 Mar;47(1):1–45. doi: 10.1128/mr.47.1.1-45.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Paul C., Rosenbusch J. P. Folding patterns of porin and bacteriorhodopsin. EMBO J. 1985 Jun;4(6):1593–1597. doi: 10.1002/j.1460-2075.1985.tb03822.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Robertson J. G., Lyttleton P. Coated and smooth vesicles in the biogenesis of cell walls, plasma membranes, infection threads and peribacteroid membranes in root hairs and nodules of white clover. J Cell Sci. 1982 Dec;58:63–78. doi: 10.1242/jcs.58.1.63. [DOI] [PubMed] [Google Scholar]
  11. Robertson J. G., Lyttleton P. Division of peribacteroid membranes in root nodules of white clover. J Cell Sci. 1984 Jul;69:147–157. doi: 10.1242/jcs.69.1.147. [DOI] [PubMed] [Google Scholar]
  12. Robertson J. G., Warburton M. P., Lyttleton P., Fordyce A. M., Bullivant S. Membranes in lupin root nodules. II. Preparation and properties of peribacteroid membranes and bacteroid envelope inner membranes from developing lupin nodules. J Cell Sci. 1978 Apr;30:151–174. doi: 10.1242/jcs.30.1.151. [DOI] [PubMed] [Google Scholar]
  13. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Verma D. P., Kazazian V., Zogbi V., Bal A. K. Isolation and characterization of the membrane envelope enclosing the bacteroids in soybean root nodules. J Cell Biol. 1978 Sep;78(3):919–936. doi: 10.1083/jcb.78.3.919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Verma D. P., Nash D. T., Schulman H. M. Isolation and in vitro translation of soybean leghaemoglobin mRNA. Nature. 1974 Sep 6;251(5470):74–77. doi: 10.1038/251074a0. [DOI] [PubMed] [Google Scholar]
  16. Watson M. E. Compilation of published signal sequences. Nucleic Acids Res. 1984 Jul 11;12(13):5145–5164. doi: 10.1093/nar/12.13.5145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Wickner W. T., Lodish H. F. Multiple mechanisms of protein insertion into and across membranes. Science. 1985 Oct 25;230(4724):400–407. doi: 10.1126/science.4048938. [DOI] [PubMed] [Google Scholar]
  18. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]
  19. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 Jun 11;14(11):4683–4690. doi: 10.1093/nar/14.11.4683. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES