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

Bozhkov, PV; Suarez, MF; Filonova, LH; Daniel, G; Zamyatnin, AA; Rodriguez-Nieto, S; Zhivotovsky, B; Smertenko, A

Authors

PV Bozhkov

MF Suarez

LH Filonova

G Daniel

AA Zamyatnin

S Rodriguez-Nieto

B Zhivotovsky

A Smertenko



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.

Citation

Bozhkov, P., Suarez, M., Filonova, L., Daniel, G., Zamyatnin, A., Rodriguez-Nieto, S., …Smertenko, A. (2005). Cysteine protease mcll-Pa executes programmed cell death during plant embryogenesis. Proceedings of the National Academy of Sciences, 102(40), 14463-14468. https://doi.org/10.1073/pnas.0506948102

Journal Article Type Article
Publication Date Oct 1, 2005
Deposit Date May 15, 2007
Journal Proceedings of the National Academy of Sciences
Print ISSN 0027-8424
Electronic ISSN 1091-6490
Publisher National Academy of Sciences
Peer Reviewed Peer Reviewed
Volume 102
Issue 40
Pages 14463-14468
DOI https://doi.org/10.1073/pnas.0506948102
Keywords Embryo suspensor, Metacaspase, Nuclear degradation.