Differential Regulation of β-1,3-Glucanase Messenger RNAs in Response to Pathogen Infection

Abstract

The acidic, extracellular, glucan endo-1,3-t8-glucosidases (EC 3.2.1.39; j0-1,3-glucanases), pathogenesis-related proteins-2, -N, and -O (i.e. PR-2, PR-N, and PR-0) were purified from Nicotiana tabacum (tobacco) and their partial amino acid sequences determined. Based on these data, complementary DNA (cDNA) clones encoding the proteins were isolated. Additional cDNAs were isolated that encoded proteins approximately 90% identical with PR-2, PR-N, and PR-0. Although the proteins encoded by these cDNAs have not been identified, their deduced amino acid sequences have slightly basic or neutral calculated isoelectric points, as well as carboxy-terminal extensions. These physical characteristics are shared by the vacuolar form of ,B-1,3-glucanase and other vacuolar localized analogs of PR proteins, suggesting that the unidentified proteins may be similarly localized.A preliminary evolutionary model that separates the fl-1,3-glucanase gene family from tobacco into at least five distinct subfamilies is proposed. The expression of ,-1,3-glucanase messenger RNAs (mRNAs) in response to infection by tobacco mosaic virus was examined. Messages for the acidic glucanases were induced similarly to the mRNAs for other PR proteins. However, the basic glucanase showed a different response, suggesting that different isoforms are differentially regulated by tobacco mosaic virus infection at the mRNA level.

Differential Expression of β-1,3-Glucanase Transcripts Induced by Pathogens in the Leaves of Vitis flexuosa

“…β-1,3-glucanases genes comprise a large gene family that has been subdivided into three major classes based on their primary structures (Neale et al 1990;Payne et al 1990;Ward et al 1991). It has been reported that plants express β-1,3-glucanase genes (I, II, and III) in response to fungal and viral infections (Dobnik et al 2013;Linthorst et al 1990;Sela-Buurlage et al 1993;Ward et al 1991;Zavaliev et al 2011).…”

“…It has been reported that plants express β-1,3-glucanase genes (I, II, and III) in response to fungal and viral infections (Dobnik et al 2013;Linthorst et al 1990;Sela-Buurlage et al 1993;Ward et al 1991;Zavaliev et al 2011). In V. vinifera, 16 β-1,3-glucanases are present, but only five are basic proteins, and one of them contains both the N-and C-terminal signal peptide sequences (Jaillon et al 2007).…”

Purification and characterization of beta-1, 3-glucanase from the secretion of Simira glaziovii colleters (Rubiaceae)

“…Many of these substances are used by the plants to create adverse conditions or may attack the pathogen directly (Beart et al, 1985;Friend, 1991). Similarly to the secretion of S. glaziovii, only one soluble β-1,3-glucanase exists in celery (Stephen and Rebecca, 1993), unlike in other species of plants, where different isoforms of Chitinase and β-1,3-glucanase usually exist (Pegg and Yong, 1981;Kauffmann et al, 1987;Mauch et al, 1988;Ward et al, 1991). The detection of a β-1,3-glucanase in the S. glaziovii secretion, confirmed by enzymatic assay after a SDS-PAGE suggested that the exuded protein secretion possesses a defense role.…”

Strategies for Control of Fungal Diseases with Transgenic Plants

“…therein). Three major classes (1-111) of /3-1,3-endoglucanases are also found in this plant species (Ward et al, 1991). The class I hydrolases are localized in the plant vacuoles and are potent inhibitors of growth in vitro of many fungi.…”