Isolation and nucleotide sequence of cDNA clones encoding potato chitinase genes

LaFlamme, Daniel; Roxby, Robert

doi:10.1007/bf00016142

Cited by 28 publications

(14 citation statements)

References 7 publications

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“…The library was screened by plaque hybridization using an Eco RI fragment isolated from a partial cDNA clone of a potato chitinase, CCH4 [14]. Three positive clones, 2Chit3, 2Chit5, and 2Chit6, were obtained.…”

Section: Methodsmentioning

confidence: 99%

Molecular cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan

Chang

Horovitz²,

Culley

et al. 1995

Plant Mol Biol

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The fungicidal class I endochitinases (E.C.3.3.1.14, chitinase) are associated with the biochemical defense of plants against potential pathogens. We isolated and sequenced a genomic clone, DAH53, corresponding to a class I basic endochitinase gene in pea, Chi1. The predicted amino acid sequence of this chitinase contains a hydrophobic C-terminal domain similar to the vacuole targeting sequences of class I chitinases isolated from other plants. The pea genome contains one gene corresponding to the chitinase DAH53 probe. Chitinase RNA accumulation was observed in pea pods within 2 to 4 h after inoculation with the incompatible fungal strain Fusarium solani f. sp. phaseoli, the compatible strain F. solani f.sp. pisi, or the elicitor chitosan. The RNA accumulation was high in the basal region (lower stem and root) of both fungus challenged and wounded pea seedlings. The sustained high levels of chitinase mRNA expression may contribute to later stages of pea's non-host resistance.

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Section: Methodsmentioning

confidence: 99%

Molecular cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan

Chang

Horovitz²,

Culley

et al. 1995

Plant Mol Biol

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“…Nevertheless Y181, E244, W248, E296, and Y321 are identical in yeast ~-1,3-glucanase and all plant ~-1,3-glucanases surveyed. The two glutamates are present in the conserved sequences (Broglie eta!., 1986(Broglie eta!., , 1989; BEAN-4, bean eDNA clone (A wade, 1989; Margis-Pinheiro eta!., 1991); CUCUMBER, cucumber eDNA clone (Metraux et a!., 1989); HEVEA, Hevea brasiliensis chitinase (Jekel eta!., 1991 ); PET, petunia eDNA clone Pach 1 (Linthorst eta!., 1990a); POP-6 and POP-8, poplar eDNA clones Win 6 and Win 8 (Parsq.ns et al, 1989); POT, potato eDNA clone RU8604 (Gaynor, 1988); POT-4, potato eDNA clone CCH4 (Laflamme and Roxby, 1989); POT-28 and POT-35, potato eDNA clones BC28 and BC 35 (E. Kombrink, pers. comm.…”

Section: Catalytic Activitymentioning

confidence: 98%

“…There is considerable inter-and intraspecific variation in the length of the spacer. It is absent in the poplar enzyme WIN-8 (Parsons et al, 1989), ranges from 8 to 18 residues in tobacco chitinases and from 4 to 6 residues in potato chitinases (Gaynor, 1988;Gaynor and Unkenholz, 1989;Laflamme and Roxby, 1989).…”

Section: Class Imentioning

confidence: 98%

The Primary Structure of Plant Pathogenesis-related Glucanohydrolases and Their Genes

Meins

Sperisen

Neuhaus

et al. 1992

Plant Gene Research

112

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“…Laflamme & Roxby, 1989;Metraux et al, 1989;Parsons et al, 1989;Payne et al, 1990;Watanabe et al, 1990b;Samac et al, 1990;Zhu & Lamb, 1991 ;Watanabe et al, 1992;Kuranda & Robbins, 1991), but these sequences are not always homologous. This suggests that chitinase genes have spread through various organisms in the process of evolution and have formed several gene families.…”

Section: The Nucleotide Sequence Data Reported In This Paper Have Beementioning

confidence: 99%

Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans

Fujii

Miyashita

1993

Journal of General Microbiology

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~~One of the chitinases of Streptomyces lividans, chitinase C, was encoded by a 2 kb smaI-XhoI restriction fragment contained in the recombinant plasmid pEMJ7. DNA sequence analysis of this region revealed the presence of two open reading frames (ORFl and ORF2) which had opposite orientations. Northern analysis showed that only the mRNA complementary to ORFl was transcribed, and that this transcription was induced by chitin and repressed by glucose. ORFl showed a codon distribution typical of Streptomyces. A sequence identical to that of the Nterminus of mature secreted chitinase C was found from amino acid residue 31 in the deduced amino acid sequence of ORFl(619 amino acids), implying that ORFl encodes a pre-protein of chitinase C. The pre-protein of chitinase C consisted of four discrete domains. The 30 amino acid N-terminal sequence, domain 1, was characteristic of a signal peptide. Domain 2 consisted of 105 N-terminal amino acids of mature chitinase C, and was similar to cellulose-binding domains of several cellulases. Domain 3 (94 amino acids) showed homology with type I11 homology units of fibronectin. Domain 4, a C-terminal390 amino acid sequence, is probably the catalytic domain of the chitinase, since it exhibited identity with several other chitinolytic enzymes.

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Isolation and nucleotide sequence of cDNA clones encoding potato chitinase genes

Cited by 28 publications

References 7 publications

Molecular cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan

Molecular cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan

The Primary Structure of Plant Pathogenesis-related Glucanohydrolases and Their Genes

Multiple domain structure in a chitinase gene (chiC) of Streptomyces lividans

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