A chloroplastic protein is immunologically and functionally related to the bacterial ATP-dependent Lon protease
Desimone, M., Wessel, T., Johanningmeier, U., Wagner, E.
Institut für Biologie II, Universität Freiburg, Schänzlestr. 1, D-79104 Freiburg, Germany
The removal of defective proteins is essential for chloroplast development and maintenance of chloroplast function. It has been suggested that the turnover of abnormal proteins occurs in an energy-dependent manner. We have recently studied the degradation of active oxygen damaged Rubisco and found that its proteolysis requires ATP-hydrolysis [1,3]. However, the identity of the protease related to this degradative process remains elusive. Two ATP-dependent proteases which are homologues to bacterial proteases have been found in chloroplasts [2]. The aim of the present study is to detect chloroplastic proteins related to another energy-dependent protease of prokaryotes, the Lon protease. The combination of immunological with enzymatical evidences preliminarly suggests that a Lon homologue is present in chloroplasts.
[1] Desimone, M. et al. (1996) Plant Physiol. 111: 789-796
[2] Desimone, M. et al. (1997) Bot. Acta 110: 234-239
[3] Desimone, M. et al. (1998) Planta in press
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