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. 1997 Jul;114(3):771–778. doi: 10.1104/pp.114.3.771

A class IV chitinase is highly expressed in grape berries during ripening.

S P Robinson 1, A K Jacobs 1, I B Dry 1
PMCID: PMC158363  PMID: 9232868

Abstract

Chitinase activity increased markedly at the onset of ripening in grape (Vitis vinifera L.) berries and continued to increase throughout the sugar accumulation phase of berry development. In contrast, beta-1,3-glucanase activity was not detected in grape berries at any stage of development. Two closely related chitinase cDNAs (VvChi4A and VvChi4B) were cloned from grapes. Sequence and Southern analysis indicate that these two clones may represent alleles of the same gene. The predicted proteins are acidic and have a signal peptide followed by a cysteine-rich, chitin-binding domain and a catalytic region. An analysis of their sequences indicates that they are class IV chitinase. The deduced protein sequence of VvChi4A has a high level of identity with the 32- and 28-kD chitinases present as haze proteins in wine. Expression of VvChi4 was high in berries and low in flowers but was not detected in leaves, roots, or seeds. No expression was detected in berries 2 to 8 weeks postflowering, but expression was high 12 to 16 weeks postflowering, which coincided with sugar accumulation and an increase in chitinase activity. Constitutive expression of VvChi4 appears to be fruit-specific and induced at high levels in grapes during ripening.

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Selected References

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  1. Coombe B. G., Hale C. R. The hormone content of ripening grape berries and the effects of growth substance treatments. Plant Physiol. 1973 Apr;51(4):629–634. doi: 10.1104/pp.51.4.629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Coombe B. G. Relationship of Growth and Development to Changes in Sugars, Auxins, and Gibberellins in Fruit of Seeded and Seedless Varieties of Vitis Vinifera. Plant Physiol. 1960 Mar;35(2):241–250. doi: 10.1104/pp.35.2.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Davies C., Robinson S. P. Sugar accumulation in grape berries. Cloning of two putative vacuolar invertase cDNAs and their expression in grapevine tissues. Plant Physiol. 1996 May;111(1):275–283. doi: 10.1104/pp.111.1.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Harikrishna K., Jampates-Beale R., Milligan S. B., Gasser C. S. An endochitinase gene expressed at high levels in the stylar transmitting tissue of tomatoes. Plant Mol Biol. 1996 Mar;30(5):899–911. doi: 10.1007/BF00020802. [DOI] [PubMed] [Google Scholar]
  5. Jach G., Görnhardt B., Mundy J., Logemann J., Pinsdorf E., Leah R., Schell J., Maas C. Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J. 1995 Jul;8(1):97–109. doi: 10.1046/j.1365-313x.1995.08010097.x. [DOI] [PubMed] [Google Scholar]
  6. Leubner-Metzger G., Frundt C., Vogeli-Lange R., Meins F., Jr Class I [beta]-1,3-Glucanases in the Endosperm of Tobacco during Germination. Plant Physiol. 1995 Nov;109(3):751–759. doi: 10.1104/pp.109.3.751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Marchuk D., Drumm M., Saulino A., Collins F. S. Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products. Nucleic Acids Res. 1991 Mar 11;19(5):1154–1154. doi: 10.1093/nar/19.5.1154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Mauch F., Mauch-Mani B., Boller T. Antifungal Hydrolases in Pea Tissue : II. Inhibition of Fungal Growth by Combinations of Chitinase and beta-1,3-Glucanase. Plant Physiol. 1988 Nov;88(3):936–942. doi: 10.1104/pp.88.3.936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Meyer B., Houlné G., Pozueta-Romero J., Schantz M. L., Schantz R. Fruit-specific expression of a defensin-type gene family in bell pepper. Upregulation during ripening and upon wounding. Plant Physiol. 1996 Oct;112(2):615–622. doi: 10.1104/pp.112.2.615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Molano J., Durán A., Cabib E. A rapid and sensitive assay for chitinase using tritiated chitin. Anal Biochem. 1977 Dec;83(2):648–656. doi: 10.1016/0003-2697(77)90069-0. [DOI] [PubMed] [Google Scholar]
  11. Nakai K., Kanehisa M. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics. 1992 Dec;14(4):897–911. doi: 10.1016/S0888-7543(05)80111-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Tattersall D. B., van Heeswijck R., Høj P. B. Identification and characterization of a fruit-specific, thaumatin-like protein that accumulates at very high levels in conjunction with the onset of sugar accumulation and berry softening in grapes. Plant Physiol. 1997 Jul;114(3):759–769. doi: 10.1104/pp.114.3.759. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Terras F. R., Schoofs H. M., De Bolle M. F., Van Leuven F., Rees S. B., Vanderleyden J., Cammue B. P., Broekaert W. F. Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J Biol Chem. 1992 Aug 5;267(22):15301–15309. [PubMed] [Google Scholar]
  14. Wemmer T., Kaufmann H., Kirch H. H., Schneider K., Lottspeich F., Thompson R. D. The most abundant soluble basic protein of the stylar transmitting tract in potato (Solanum tuberosum L.) is an endochitinase. Planta. 1994;194(2):264–273. [PubMed] [Google Scholar]

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