Substrate specificity and antifungal activity of recombinant tobacco class I chitinases View Full Text


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Article Info

DATE

2001-03

AUTHORS

Vivian Suarez, Christian Staehelin, Rafael Arango, Hauke Holtorf, Jan Hofsteenge, Frederick Meins

ABSTRACT

Endochitinases contribute to the defence response of plants against chitin-containing pathogens. The vacuolar class I chitinases consist of an N-terminal cysteine-rich domain (CRD) linked by a glycine-threonine-rich spacer with 4-hydroxylated prolyl residues to the catalytic domain. We examined the functional role of the CRD and spacer region in class I chitinases by comparing wild-type chitinase A (CHN A) of Nicotianatabacum with informative recombinant forms. The chitinases were expressed in transgenic N. sylvestris plants, purified to near homogeneity, and their structures confirmed by mass spectrometry and partial sequencing. The enzymes were tested for their substrate preference towards chitin, lipo-chitooligosaccharide Nod factors of Rhizobium, and bacterial peptidoglycans (lysozyme activity) as well as for their capacity to inhibit hyphal growth of Trichoderma viride. Deletion of the CRD and spacer alone or in combination resulted in a modest <50% reduction of hydrolytic activity relative to CHN A using colloidal chitin or M. lysodeikticus walls as substrates; whereas, antifungal activity was reduced by up to 80%. Relative to CHN A, a variant with two spacers in tandem, which binds chitin, showed very low hydrolytic activity towards chitin and Nod factors, but comparable lysozyme activity and enhanced antifungal activity. Neither hydrolytic activity, substrate specificity nor antifungal activity were strictly correlated with the CRD-mediated capacity to bind chitin. This suggests that the presence of the chitin-binding domain does not have a major influence on the functions of CHN A examined. Moreover, the results with the tandem-spacer variant raise the possibility that substantial chitinolytic activity is not essential for inhibition of T. viride growth by CHN A. More... »

PAGES

609-618

References to SciGraph publications

  • 1996-06. A revised nomenclature for chitinase genes in PLANT MOLECULAR BIOLOGY REPORTER
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  • 1995-09. Kinetics of prolyl hydroxylation, intracellular transport and C-terminal processing of the tobacco vacuolar chitinase in PLANTA
  • 1994-08-01. Enhanced Protection Against Fungal Attack by Constitutive Co–expression of Chitinase and Glucanase Genes in Transgenic Tobacco in NATURE BIOTECHNOLOGY
  • 1990-08. The effect of ethylene on the cell-type-specific and intracellular localization of β-1,3-glucanase and chitinase in tobacco leaves in PLANTA
  • 1992-04. The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin in MOLECULAR GENETICS AND GENOMICS
  • 1992-11. Regulated inactivation of homologous gene expression in transgenic Nicotiana sylvestris plants containing a defense-related tobacco chitinase gene in MOLECULAR GENETICS AND GENOMICS
  • 1995-02. Synergistic activity of chitinases and β-1,3-glucanases enhances fungal resistance in transgenic tomato plants in EUPHYTICA
  • 1992. The Primary Structure of Plant Pathogenesis-related Glucanohydrolases and Their Genes in GENES INVOLVED IN PLANT DEFENSE
  • 1991-01. High-level expression of a tobacco chitinase gene in Nicotiana sylvestris. Susceptibility of transgenic plants to Cercospora nicotianae infection in PLANT MOLECULAR BIOLOGY
  • 1986-11-01. Plant chitinases are potent inhibitors of fungal growth in NATURE
  • 1996-06. Characterzation of chitinases able to rescue somatic embryos of the temperature-sensitive carrot variantts11 in PLANT MOLECULAR BIOLOGY
  • 1991-01. Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex in PLANTA
  • 1981. Fungal Cell Walls: A Survey in PLANT CARBOHYDRATES II
  • 1997-06-01. Structural and Evolutionary Relationships Among Chitinases of Flowering Plants in JOURNAL OF MOLECULAR EVOLUTION
  • 1990-03. Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain in PLANT MOLECULAR BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1023/a:1010619421524

    DOI

    http://dx.doi.org/10.1023/a:1010619421524

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11414619


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    43 schema:description Endochitinases contribute to the defence response of plants against chitin-containing pathogens. The vacuolar class I chitinases consist of an N-terminal cysteine-rich domain (CRD) linked by a glycine-threonine-rich spacer with 4-hydroxylated prolyl residues to the catalytic domain. We examined the functional role of the CRD and spacer region in class I chitinases by comparing wild-type chitinase A (CHN A) of Nicotianatabacum with informative recombinant forms. The chitinases were expressed in transgenic N. sylvestris plants, purified to near homogeneity, and their structures confirmed by mass spectrometry and partial sequencing. The enzymes were tested for their substrate preference towards chitin, lipo-chitooligosaccharide Nod factors of Rhizobium, and bacterial peptidoglycans (lysozyme activity) as well as for their capacity to inhibit hyphal growth of Trichoderma viride. Deletion of the CRD and spacer alone or in combination resulted in a modest <50% reduction of hydrolytic activity relative to CHN A using colloidal chitin or M. lysodeikticus walls as substrates; whereas, antifungal activity was reduced by up to 80%. Relative to CHN A, a variant with two spacers in tandem, which binds chitin, showed very low hydrolytic activity towards chitin and Nod factors, but comparable lysozyme activity and enhanced antifungal activity. Neither hydrolytic activity, substrate specificity nor antifungal activity were strictly correlated with the CRD-mediated capacity to bind chitin. This suggests that the presence of the chitin-binding domain does not have a major influence on the functions of CHN A examined. Moreover, the results with the tandem-spacer variant raise the possibility that substantial chitinolytic activity is not essential for inhibition of T. viride growth by CHN A.
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