Abstract

Survival of pseudomonads during plant colonization may involve bacterial catalases to degrade the hydrogen peroxide produced by the plant. The specific activities of catalases in lysates from two saprophytic isolates of Pseudomonas putida and Pseudomonas fluorescens and three races of Pseudomonas syringae pv. glycinea were similar. To explore the location of the bacterial catalases, cells of the pathogenic and saprophytic pseudomonads were treated with chloroform, which is reported to release periplasmic proteins. Although catalase was released by chloroform treatment, the cytoplasmic enzymes isocitrate dehydrogenase, superoxide dismutase, and glucose-6-phosphate dehydrogenase were also detected. These proteins may have come from lysis of a small proportion of the cells rather than the periplasm. Water treatment of cells also released amounts of protein similar to those derived from chloroform treatment. Similar responses were found from both pathogenic and saprophytic strains. The release of catalase and proteins from the leaf pathogen P. syringae pv. glycinea race 0 and the root-associated saprophyte P. putida decreased as the cultures aged. With P. putida and P. syringae pv. glycinea race 0, the single isozyme of catalase released by water and chloroform treatment also was detected in lysates. Additional catalase isozymes were present in lysates as the cultures aged.Key words: periplasmic proteins, survival.

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