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Cysteine protease mcll-Pa executes programmed cell death during plant embryogenesis.

Bozhkov, P. V. and Suarez, M. F. and Filonova, L. H. and Daniel, G. and Zamyatnin, A. A. and Rodriguez-Nieto, S. and Zhivotovsky, B. and Smertenko, A. (2005) 'Cysteine protease mcll-Pa executes programmed cell death during plant embryogenesis.', Proceedings of the National Academy of Sciences of the United States Of America., 102 (40). pp. 14463-14468.

Abstract

Programmed cell death (PCD) is indispensable for eukaryotic development. In animals, PCD is executed by the caspase family of cysteine proteases. Plants do not have close homologues of caspases but possess a phylogenetically distant family of cysteine proteases named metacaspases. The cellular function of metacaspases in PCD is unknown. Here we show that during plant embryogenesis, metacaspase mcII-Pa translocates from the cytoplasm to nuclei in terminally differentiated cells that are destined for elimination, where it colocalizes with the nuclear pore complex and chromatin, causing nuclear envelope disassembly and DNA fragmentation. The cell-death function of mcII-Pa relies on its cysteine-dependent arginine-specific proteolytic activity. Accordingly, mutation of catalytic cysteine abrogates the proteolytic activity of mcII-Pa and blocks nuclear degradation. These results establish metacaspase as an executioner of PCD during embryo patterning and provide a functional link between PCD and embryogenesis in plants. Although mcII-Pa and metazoan caspases have different substrate specificity, they serve a common function during development, demonstrating the evolutionary parallelism of PCD pathways in plants and animals.

Item Type:Article
Keywords:Embryo suspensor, Metacaspase, Nuclear degradation.
Full text:Full text not available from this repository.
Publisher Web site:http://dx.doi.org/10.1073/pnas.0506948102
Record Created:15 May 2007
Last Modified:06 Jul 2009 10:32

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