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. 1997 Jul;114(3):981–988. doi: 10.1104/pp.114.3.981

Effects of a mechanical stimulation of localization of annexin-like proteins in Bryonia dioica internodes.

C Thonat 1, C Mathieu 1, M Crevecoeur 1, C Penel 1, T Gaspar 1, N Boyer 1
PMCID: PMC158386  PMID: 9232879

Abstract

Mechanical stimulation exerted by rubbing a young internode of Bryonia dioica plants inhibits its growth. Previous cellular and biochemical studies showed that this growth inhibition is associated with Ca(2+) redistribution and profound modifications of plasma membrane characteristics. We extracted and purified Ca(2+)-dependent phospholipid-binding proteins from B. dioica internodes. Two main proteins, p33 and p35, and other minor bands were isolated and identified as annexin-like proteins because of their biochemical properties and their cross-reactions with antibodies against maize (Zea mays L.) annexins. Rabbit antiserum was obtained by injection of B. dioica p35. This antiserum was used for the immunocytolocalization of annexin-like proteins in internode parenchyma cells. It appeared that the distribution of annexin-like proteins was different before and 30 min after the mechanical stimulation. Western analysis of proteins in membrane fractions after separation by free-flow electrophoresis showed that p35 was present in most fractions, whereas p33 appeared mainly in plasmalemma-enriched fractions after the mechanical stimulation. It is hypothesized that a subcellular redistribution of these proteins might be involved in growth inhibition by mechanical stress.

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Selected References

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  1. Blackbourn H. D., Barker P. J., Huskisson N. S., Battey N. H. Properties and partial protein sequence of plant annexins. Plant Physiol. 1992 Jul;99(3):864–871. doi: 10.1104/pp.99.3.864. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Boyer N., Desbiez M. O., Hofinger M., Gaspar T. Effect of Lithium on Thigmomorphogenesis in Bryonia dioica Ethylene Production and Sensitivity. Plant Physiol. 1983 Jun;72(2):522–525. doi: 10.1104/pp.72.2.522. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  4. Creutz C. E. The annexins and exocytosis. Science. 1992 Nov 6;258(5084):924–931. doi: 10.1126/science.1439804. [DOI] [PubMed] [Google Scholar]
  5. Crumpton M. J., Dedman J. R. Protein terminology tangle. Nature. 1990 May 17;345(6272):212–212. doi: 10.1038/345212a0. [DOI] [PubMed] [Google Scholar]
  6. De Jaegher G., Boyer N. Specific Inhibition of Lignification in Bryonia dioica: Effects on Thigmomorphogenesis. Plant Physiol. 1987 May;84(1):10–11. doi: 10.1104/pp.84.1.10. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Galaud J. P., Lareyre J. J., Boyer N. Isolation, sequencing and analysis of the expression of Bryonia calmodulin after mechanical perturbation. Plant Mol Biol. 1993 Nov;23(4):839–846. doi: 10.1007/BF00021538. [DOI] [PubMed] [Google Scholar]
  8. Haigler H. T., Fitch J. M., Jones J. M., Schlaepfer D. D. Two lipocortin-like proteins, endonexin II and anchorin CII, may be alternate splices of the same gene. Trends Biochem Sci. 1989 Feb;14(2):48–50. doi: 10.1016/0968-0004(89)90041-8. [DOI] [PubMed] [Google Scholar]
  9. Hochstrasser D. F., Harrington M. G., Hochstrasser A. C., Miller M. J., Merril C. R. Methods for increasing the resolution of two-dimensional protein electrophoresis. Anal Biochem. 1988 Sep;173(2):424–435. doi: 10.1016/0003-2697(88)90209-6. [DOI] [PubMed] [Google Scholar]
  10. Huber R., Römisch J., Paques E. P. The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 1990 Dec;9(12):3867–3874. doi: 10.1002/j.1460-2075.1990.tb07605.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kaetzel M. A., Hazarika P., Dedman J. R. Differential tissue expression of three 35-kDa annexin calcium-dependent phospholipid-binding proteins. J Biol Chem. 1989 Aug 25;264(24):14463–14470. [PubMed] [Google Scholar]
  12. 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]
  13. Lennette D. A. An improved mounting medium for immunofluorescence microscopy. Am J Clin Pathol. 1978 Jun;69(6):647–648. doi: 10.1093/ajcp/69.6.647. [DOI] [PubMed] [Google Scholar]
  14. Lin H. C., Südhof T. C., Anderson R. G. Annexin VI is required for budding of clathrin-coated pits. Cell. 1992 Jul 24;70(2):283–291. doi: 10.1016/0092-8674(92)90102-i. [DOI] [PubMed] [Google Scholar]
  15. Poovaiah B. W., Reddy A. S. Calcium and signal transduction in plants. CRC Crit Rev Plant Sci. 1993;12(3):185–211. doi: 10.1080/07352689309701901. [DOI] [PubMed] [Google Scholar]
  16. Rojas E., Pollard H. B., Haigler H. T., Parra C., Burns A. L. Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J Biol Chem. 1990 Dec 5;265(34):21207–21215. [PubMed] [Google Scholar]
  17. Sandelius A. S., Penel C., Auderset G., Brightman A., Millard M., Morré D. J. Isolation of highly purified fractions of plasma membrane and tonoplast from the same homogenate of soybean hypocotyls by free-flow electrophoresis. Plant Physiol. 1986 May;81(1):177–185. doi: 10.1104/pp.81.1.177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sarafian T., Pradel L. A., Henry J. P., Aunis D., Bader M. F. The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C. J Cell Biol. 1991 Sep;114(6):1135–1147. doi: 10.1083/jcb.114.6.1135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Smallwood M., Keen J. N., Bowles D. J. Purification and partial sequence analysis of plant annexins. Biochem J. 1990 Aug 15;270(1):157–161. doi: 10.1042/bj2700157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Thonat C., Boyer N., Penel C., Courduroux J. C., Gaspar T. Cytological indication of the involvement of calcium and calcium-related proteins in the early responses of Bryonia dioica to mechanical stimulus. Protoplasma. 1993;176(3-4):133–137. doi: 10.1007/BF01378949. [DOI] [PubMed] [Google Scholar]
  21. 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]

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