Degradation of Tobacco Pathogenesis-related Proteins : Evidence for Conserved Mechanisms of Degradation of Pathogenesis-related Proteins in Plants

Overview

Journal Plant Physiol

Specialty Physiology

Date 1991 Feb 1

PMID 16668027

Citations 14

Authors

I Rodrigo

P Vera

L C van Loon

V Conejero

Affiliations

Soon will be listed here.

Abstract

Tobacco (Nicotiana tabacum L.) leaves were found to contain an extracellular proteinase that endoproteolytically cleaves tobacco pathogenesis-related (PR) proteins. This proteinase was partially purified from tobacco leaves and characterized as an aspartyl proteinase with a pH optimum around pH 3 and a molecular mass of 36,000 to 40,000 daltons. In vitro, the enzyme cleaved purified tobacco and tomato PR proteins into discrete fragments. The characteristics of this proteinase were similar to pepsin and identical to those displayed by a previously described tomato 37-kilodalton aspartyl proteinase active against tomato PR proteins (I Rodrigo, P Vera, V Conejero [1989] Eur J Biochem 184: 663-669), suggesting that these extracellular proteases could play a role in a conserved mechanism for PR protein turnover in plants.

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