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

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 funct...

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Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 102; no. 40; pp. 14463 - 14468
Main Authors:	Bozhkov, P.V, Suarez, M.F, Filonova, L.H, Daniel, G, Zamyatnin, A.A. Jr, Rodriguez-Nieto, S, Zhivotovsky, B, Smertenko, A
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences 04-10-2005 National Acad Sciences
Subjects:	apoptosis Apoptosis - physiology Base Sequence Biological Sciences Cell free system Cell lines Cell nucleus Cell Nucleus - physiology Cell Nucleus - ultrastructure Chemical suspensions Chromatin Cysteine Endopeptidases - genetics Cysteine Endopeptidases - metabolism cysteine proteinases Cytoplasm DNA Fragmentation - physiology Embryogenesis Embryonic cells Embryos enzyme activity Immunoblotting immunocytochemistry Immunohistochemistry In Situ Nick-End Labeling Kinetics Medicin och hälsovetenskap Microscopy, Electron Microscopy, Fluorescence Molecular Sequence Data Nuclear membrane Picea - embryology Picea abies protein transport Sequence Analysis, DNA Substrate Specificity
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 Communicated by Ronald R. Sederoff, North Carolina State University, Raleigh, NC, August 16, 2005 Abbreviations: PCD, programmed cell death; cmk, chloromethyl ketone. Data deposition: The sequence reported in this paper has been deposited in the EMBL database [accession no. AJ534970 (mcII-Pa)]. P.V.B., M.F.S., and L.H.F. contributed equally to this work. To whom correspondence should be addressed. E-mail: peter.bozhkov@vbsg.slu.se. Author contributions: P.V.B., M.F.S., and A.S. designed research; P.V.B., M.F.S., L.H.F., G.D., A.A.Z., S.R.-N., and A.S. performed research; G.D. and B.Z. contributed new reagents/analytic tools; P.V.B., M.F.S., L.H.F., and A.S. analyzed data; and P.V.B., B.Z., and A.S. wrote the paper.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.0506948102