Processing of the pectate lyase Pell by extracellular proteases of Erwinia chrysanthemi 3937

• Published in: Molecular microbiology Vol. 29; no. 6; pp. 1459 - 1469
• Main Authors: Shevchik, Vladimir E, Boccara, Martine, Vedel, Regine, Hugouvieux-cotte-Pattat, Nicole
• Format: Journal Article
• Language: English
• Published: Oxford Blackwell Publishing Ltd 01.09.1998
• ISSN: 0950-382X; 1365-2958
• DOI: 10.1046/j.1365-2958.1998.01028.x

Erwinia chrysanthemi causes soft rot on various plants. The maceration of plant tissues is mainly due to the action of endopectate lyases. The E. chrysanthemi strain 3937 produces eight endopectate lyases (PelA, PelB, PelC, PelD, PelE, PelI, PelL and PelZ) that are secreted by the Out pathway. The necrotic response elicited by the wild-type E. chrysanthemi strain on tobacco leaves is due to an extracellular protein secreted by the Out machinery. Purification of the active factor revealed that it corresponds to a pectate lyase presenting immunological cross-reaction with PelI. Analysis of pelI and out mutants indicated that the necrosis-inducing pectate lyase results from a post-translational modification of PelI occurring extracellularly both in culture media and in planta. This modification consists of the cleavage of 97 N-terminal amino acids by the extracellular proteases of E. chrysanthemi. The enzymatic properties of the maturated form, PelI-3, are not, or only weakly, modified. However, this maturation gives rise to a small size and basic form that is active as a defence elicitor in plants.