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Metabolism and Enzymology

Tobacco Mesophyll Protoplasts Synthesize 1,3--Glucanase, Chitinases, and "Osmotins" during in Vitro Culture

Université de Perpignan, Laboratoire de Physiologie Végétale, Avenue de Villeneuve, 66025 Perpignan Cédex, France, Institut de Biologie Molécularie des Plantes du CNRS, Université Louis Pasteur, 12, Rue du Général Zimmer, 67084 Strasbourg Cédex, France

Tobacco (Nicotiana tabacum) mesophyll protoplasts synthesize six basic proteins (a, a', a₁, b, b', and c) which are undetectable in the leaf and whose synthesis is reduced by auxin (Y Meyer, L Aspart, Y Chartier [1984] Plant Physiol 75: 1027-1033). Polypeptides a, a', and a₁ were shown to have similar mobilities on two-dimensional electrophoresis as one 1,3--glucanase and two chitinases from tobacco mosaic virus-infected leaves. In immunoblotting experiments, polypeptide a was recognized by specific antibodies raised against the 1,3--glucanase and a' and a₁ reacted with anti-chitinase antibodies. Similarly, b and b' comigrated with osmotin and its neutral counterpart, two proteins characteristic of salt-adapted tobacco cells, and reacted with anti-osmotin antibodies. In addition it has been shown that 1,3--glucanase and chitinase activities increased at the same time as a, a', and a₁ accumulated in cultivated protoplasts. Finally, polypeptide c was also detected in tobacco mosaic virus-infected leaves but could not be identified as any of the pathogenesis-related proteins characterized so far in tobacco. Thus, cultivated tobacco protoplasts synthesize and accumulate typical stress proteins.

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