Feb 1, 1989

Isolation of a complementary DNA encoding a chitinase with structural homology to a bifunctional lysozyme/chitinase

Proceedings of the National Academy of Sciences of the United States of America
J P MetrauxJ Ryals

Abstract

An extracellular, acidic chitinase was purified to homogeneity from tobacco necrosis virus-infected leaves of Cucumis sativis. The amino acid sequences of the intact protein and of peptides isolated following endoproteinase Lys-C digestion, cyanogen bromide cleavage, and trypsin digestion were determined. Oligonucleotide probes derived from this sequence were used to isolate a cDNA clone encoding this protein. No significant homology was found between this chitinase and either the basic chitinase isolated from bean or tobacco or the chitinase isolated from Serratia marcescens; however, strong homology was found between the cucumber chitinase and a lysozyme/chitinase from Parthenocissus quinquifolia. The induction of the protein by tobacco necrosis virus infection or salicylate was found to be at the level of RNA accumulation. Genomic Southern analysis indicates that a single gene in the cucumber genome encodes this protein.

  • References9
  • Citations70

References

  • References9
  • Citations70

Mentioned in this Paper

Tumor Virus Infections
Tobacco
Genome
Extracellular
Serratia marcescens
Genes, Spliced
Lysozyme Test
Plants, Toxic
Cytokinesis of the Fertilized Ovum
Endochitinase

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