PEL-C is the Major Pectate Lyase Produced by Erwinia Chrysanthemi (EC16) in Vitro and in Plant Tissue

Abstract

Genetic data have revealed an important role of E. chrysanthemi (EC16) pectate lyases in plant tissue maceration. This bacterium, like other E. chrysanthemi strains, produces several pectate lyases, some of which are encoded by different structural genes. However, little is currently known about the distribution of each of the pectate lyases and their regulation, export, and effects on plant tissue. To better understand the physiology of production and ecological significance, we purified three extracellular pectate lyases (PEL-A, PEL-B and PEL-C) from strain EC16 and produced antibody against the purified PEL-C. Anti-PEL-C antibody was highly specific since it did not precipitate purified PEL-A or PEL-B or inhibit their enzymatic activities. These observations were confirmed by using pectate lyases produced by E. coli strains carrying cloned pel genes of EC16. The antibody completely blocked the activity of PEL-C produced by E. coli/pPL742, yet it had no effect on PEL-A and PEL-B activities in E. coli/pPL3 and PEL-A activity in E. coli/pAKC307. Antigen titration data indicated that PEL-C contributed about 50–60% of the total pectate lyase activity produced by E. chrysanthemi (EC16) in potato tuber tissue and in culture under induced conditions.KeywordsPlant PathologyPlant TissueStructural GenePathogenic BacteriumGenetic DataThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.