Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1997 Jul;114(3):1071–1076. doi: 10.1104/pp.114.3.1071

A cDNA clone highly expressed in ripe banana fruit shows homology to pectate lyases.

E Dominguez-Puigjaner 1, I LLop 1, M Vendrell 1, S Prat 1
PMCID: PMC158396  PMID: 9232883

Abstract

A cDNA clone (Ban17), encoding a protein homologous to pectate lyase, has been isolated from a cDNA library from climacteric banana fruit by means of differential screening. Northern analysis showed that Ban17 mRNA is first detected in early climacteric fruit, reaches a steady-state maximum at the climacteric peak, and declines thereafter in overripe fruit. Accumulation of the Ban17 transcript can be induced in green banana fruit by exogenous application of ethylene. The demonstrates that expression of this gene is under hormonal control, its induction being regulated by the rapid increase in ethylene production at the onset of ripening. The deduced amino acid sequence derived from the Ban17 cDNA shares significant identity with pectate lyases from pollen and plant pathogenic bacteria of the genus Erwinia. Similarity to bacterial pectate lyases that were proven to break down the pectic substances of the plant cell wall suggest that Ban17 might play a role in the loss of mesocarp firmness during fruit ripening.

Full Text

The Full Text of this article is available as a PDF (2.4 MB).

Selected References

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

  1. Amasino R. M. Acceleration of nucleic acid hybridization rate by polyethylene glycol. Anal Biochem. 1986 Feb 1;152(2):304–307. doi: 10.1016/0003-2697(86)90413-6. [DOI] [PubMed] [Google Scholar]
  2. Budelier K. A., Smith A. G., Gasser C. S. Regulation of a stylar transmitting tissue-specific gene in wild-type and transgenic tomato and tobacco. Mol Gen Genet. 1990 Nov;224(2):183–192. doi: 10.1007/BF00271551. [DOI] [PubMed] [Google Scholar]
  3. Carpita N. C., Gibeaut D. M. Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J. 1993 Jan;3(1):1–30. doi: 10.1111/j.1365-313x.1993.tb00007.x. [DOI] [PubMed] [Google Scholar]
  4. Dellapenna D., Lashbrook C. C., Toenjes K., Giovannoni J. J., Fischer R. L., Bennett A. B. Polygalacturonase Isozymes and Pectin Depolymerization in Transgenic rin Tomato Fruit. Plant Physiol. 1990 Dec;94(4):1882–1886. doi: 10.1104/pp.94.4.1882. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Giovannoni J. J., DellaPenna D., Bennett A. B., Fischer R. L. Expression of a chimeric polygalacturonase gene in transgenic rin (ripening inhibitor) tomato fruit results in polyuronide degradation but not fruit softening. Plant Cell. 1989 Jan;1(1):53–63. doi: 10.1105/tpc.1.1.53. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gross K. C., Wallner S. J. Degradation of Cell Wall Polysaccharides during Tomato Fruit Ripening. Plant Physiol. 1979 Jan;63(1):117–120. doi: 10.1104/pp.63.1.117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Henrissat B., Heffron S. E., Yoder M. D., Lietzke S. E., Jurnak F. Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol. 1995 Mar;107(3):963–976. doi: 10.1104/pp.107.3.963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hinton J. C., Sidebotham J. M., Gill D. R., Salmond G. P. Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia carotovora subspecies carotovora belong to different gene families. Mol Microbiol. 1989 Dec;3(12):1785–1795. doi: 10.1111/j.1365-2958.1989.tb00164.x. [DOI] [PubMed] [Google Scholar]
  9. Keen N. T., Tamaki S. Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli. J Bacteriol. 1986 Nov;168(2):595–606. doi: 10.1128/jb.168.2.595-606.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Koch J. L., Nevins D. J. Tomato fruit cell wall : I. Use of purified tomato polygalacturonase and pectinmethylesterase to identify developmental changes in pectins. Plant Physiol. 1989 Nov;91(3):816–822. doi: 10.1104/pp.91.3.816. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lietzke S. E., Yoder M. D., Keen N. T., Jurnak F. The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi. Plant Physiol. 1994 Nov;106(3):849–862. doi: 10.1104/pp.106.3.849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lincoln J. E., Cordes S., Read E., Fischer R. L. Regulation of gene expression by ethylene during Lycopersicon esculentum (tomato) fruit development. Proc Natl Acad Sci U S A. 1987 May;84(9):2793–2797. doi: 10.1073/pnas.84.9.2793. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Prat S., Willmitzer L., Sánchez-Serrano J. J. Nuclear proteins binding to a cauliflower mosaic virus 35S truncated promoter. Mol Gen Genet. 1989 Jun;217(2-3):209–214. doi: 10.1007/BF02464883. [DOI] [PubMed] [Google Scholar]
  14. Rafnar T., Griffith I. J., Kuo M. C., Bond J. F., Rogers B. L., Klapper D. G. Cloning of Amb a I (antigen E), the major allergen family of short ragweed pollen. J Biol Chem. 1991 Jan 15;266(2):1229–1236. [PubMed] [Google Scholar]
  15. Rogers H. J., Harvey A., Lonsdale D. M. Isolation and characterization of a tobacco gene with homology to pectate lyase which is specifically expressed during microsporogenesis. Plant Mol Biol. 1992 Nov;20(3):493–502. doi: 10.1007/BF00040608. [DOI] [PubMed] [Google Scholar]
  16. Tamaki S. J., Gold S., Robeson M., Manulis S., Keen N. T. Structure and organization of the pel genes from Erwinia chrysanthemi EC16. J Bacteriol. 1988 Aug;170(8):3468–3478. doi: 10.1128/jb.170.8.3468-3478.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Taniguchi Y., Ono A., Sawatani M., Nanba M., Kohno K., Usui M., Kurimoto M., Matuhasi T. Cry j I, a major allergen of Japanese cedar pollen, has pectate lyase enzyme activity. Allergy. 1995 Jan;50(1):90–93. doi: 10.1111/j.1398-9995.1995.tb02489.x. [DOI] [PubMed] [Google Scholar]
  18. Themmen A. P., Tucker G. A., Grierson D. Degradation of isolated tomato cell walls by purified polygalacturonase in vitro. Plant Physiol. 1982 Jan;69(1):122–124. doi: 10.1104/pp.69.1.122. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tieman D. M., Harriman R. W., Ramamohan G., Handa A. K. An Antisense Pectin Methylesterase Gene Alters Pectin Chemistry and Soluble Solids in Tomato Fruit. Plant Cell. 1992 Jun;4(6):667–679. doi: 10.1105/tpc.4.6.667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Turcich M. P., Hamilton D. A., Mascarenhas J. P. Isolation and characterization of pollen-specific maize genes with sequence homology to ragweed allergens and pectate lyases. Plant Mol Biol. 1993 Dec;23(5):1061–1065. doi: 10.1007/BF00021820. [DOI] [PubMed] [Google Scholar]
  21. Wing R. A., Yamaguchi J., Larabell S. K., Ursin V. M., McCormick S. Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia. Plant Mol Biol. 1990 Jan;14(1):17–28. doi: 10.1007/BF00015651. [DOI] [PubMed] [Google Scholar]
  22. Yoder M. D., Jurnak F. The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism). Plant Physiol. 1995 Feb;107(2):349–364. doi: 10.1104/pp.107.2.349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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 Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES