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JXB Advance Access originally published online on March 12, 2004
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Journal of Experimental Botany, Vol. 55, No. 398, pp. 889-897, April 1, 2004
© 2004 Oxford University Press


Regulation of Growth, Development and Whole Organism Physiology

Caspase-like activity in the seedlings of Pisum sativum eliminates weaker shoots during early vegetative development by induction of cell death

Received 19 June 2003; Accepted 24 December 2003

Beatrice Belenghi, Mazal Salomon and Alex Levine*

Department of Plant Sciences, The Hebrew University of Jerusalem, Givat-Ram Campus, Jerusalem 91904, Israel

* To whom correspondence should be addressed. Fax: +972 2 658 4425. E-mail:alexl{at}cc.huji.ac.il

Activation of aspartate-specific cysteine proteases (caspases) plays a crucial role in programmed cell death (PCD) in animals. Although to date caspases have not been identified in plants, caspase-like activity was described in tobacco during a hypersensitive response to pathogens and in Arabidopsis and tomato cell cultures during chemical-induced PCD. Caspase-like activity was also detected in the course of plant development during petal senescence and endosperm PCD. It is shown here that caspase-like proteases play a crucial role in the developmental cell death of secondary shoots of pea seedlings that emerge after removal of the epicotyl. Caspase-like activity was induced in senescing secondary shoots, but not in dominant growing shoots, in contrast to the papain-like cysteine protease activity that was stronger in the dominant shoot. Revitalization of the senescing shoot by cutting of the dominant shoot reduced the caspase-like activity. Injection of caspase or cysteine protease inhibitors into the remaining epicotyl tissue suppressed the death of the secondary shoots, producing seedlings with two equal shoots. These results suggest that shoot selection in pea seedlings is controlled by PCD, through the activation of caspase-like proteases.

Key words: Apical dominance, cysteine proteases, epicotyl, senescence, shoot development.


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