Molecular characterization of a pea ?-1,3-glucanase induced by Fusarium solani and chitosan challenge

Abstract

beta-glucanases are prominent proteins in pea endocarp tissue responding to fungal infection. We have cloned and sequenced a partial pea cDNA clone, pPIG312, corresponding to a beta-1,3-glucanase in pea pods challenged with the incompatible pathogen Fusarium solani f. sp. phaseoli. The insert from the partial pea cDNA was used to probe a genomic library derived from pea leaves of the same cultivar. One of the genomic clones, pPIG4-3, contained the complete coding sequence for a mature beta-1,3-glucanase protein. The predicted amino acid sequence of the pea beta-1,3-glucanase has 78% identity to bean beta-1,3-glucanase, 62% and 60% to two tobacco beta-1,3-glucanases, 57% to soybean beta-1,3-glucanase, 51% to barley beta-1,3-glucanase, and 48% to barley beta-1,3-1,4-glucanase. Genomic Southern analysis indicates that the pea genome contains only one beta-1,3-glucanase gene corresponding to the probe used in this study. Accumulation of beta-1,3-glucanase mRNA homologous with the pPIG312 probe was detected in pea pods within 4 to 8 h after challenge with F. solani f. sp. phaseoli, f. sp. pisi, a compatible strain, or the elicitor, chitosan. In the incompatible reaction, mRNA accumulation remained high for 48h, whereas it rapidly decreased in the compatible reaction. After fungal inoculation of whole pea seedlings, the enhanced mRNA accumulation occurred mainly in the basal region (lower stem and root). This beta-1,3-glucanase mRNA was constitutively expressed in the roots of pea seedlings.(ABSTRACT TRUNCATED AT 250 WORDS)

Effects of transgene products on honey bees (Apis mellifera) and bumblebees (Bombus sp.)

“…Neuhaus et al, 1992;Chang et al, 1992;Gottschalk et al, 1998). They have also been isolated from micro-organisms (e.g.…”

The Matrix Metalloproteinase Gene GmMMP2 Is Activated in Response to Pathogenic Infections in Soybean

“…The first group includes enzymes involved in the biosynthesis of antimicrobial compounds called phytoalexins, the secondary metabolites toxic to some pathogenic microorganisms (Schmelzer et al, 1984;Schmidt et al, 1984;Welle and Grisebach, 1988;Schopfer et al, 1998). The second group consists of carbohydrolases such as chitinases and ␤-1,3-glucanases, which lyse cell walls of invading fungi, thereby inhibiting the growth of the invaders (Chang et al, 1992;Okinaka et al, 1995). The third group contains a number of Cys-rich proteins such as proteinase inhibitors and ␥-thinion-like proteins called defensins (Broekaert et al, 1995).…”

cDNA Clones Encoding 1,3-β-Glucanase and a Fimbrin-Like Cytoskeletal Protein Are Induced by Al Toxicity in Wheat Roots

“…The deduced polypeptide contained 461 amino acids (Fig. l), the first 25 of which represent a putative signal peptide that is enriched in neutral and hydrophobic amino acids typical of eukaryotic signal sequences (Von Heijne, 1983 acid sequence of T. aestivum (Ta) 1,3-P-glucanases was aligned with the following 1,3-P-glucanases: B. napus (Bn), A. thaliana (At) (Hird et al, 1993), C V and CII from barley (Hordeum vulgare) (Hv-CV and Hv-CII) (Xu et ai., 1992), tobacco (Nicotiana tabacum) (Nt-1, and Nt-2) (Linthorst, 1991), and pea (Pisum sativum) (Ps) (Chang et al, 1992). Amino acid residues denoted with an asterisk (*) are thought to participate in the enzyme active site.…”

“…It exhibits similarity to the H. vulgare neutral GV and the basic GII 1,3-P-glucanases (35 and 37% amino acid identity, respectively) (Xu et al, 1992;Malehorn et al, 1993), with two acidic tobacco 1,3-p-glucanases (32% amino acid identity) (Linthorst, 1991), and with the slightly basic pea 1,3-P-glucanase (32% identity) (Chang et al, 1992). The wheat protein is also similar to two basic 1,3-p-glucanases from B. napus and Arabidopsis (33% identity, Hird et al, 1993) in both size and the presence of the long amino acid extension at the C-terminal end.…”