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Histones effect plant mitochondria.

HISTONES EFFECT PLANT MITOCHONDRIA. LINDA A. MAJOR AND ROGER A. SAUTERER, DEPT. OF BIOLOGY, JACKSONVILLE STATE UNIVERSITY, JACKSONVILLE, AL 36265.

The genome is continuously exposed to DNA damaging agents that activate the DNA damage response to either repair the DNA or induce apoptosis. During the early DNA damage response, the chromatin compaction around damaged sites is relaxed through specific core histone modifications and displacement of the linker histone H1. In mammalian cells, studies suggest that displaced histones enter the cytoplasm and bind to mitochondria, leading to the permeabilization of the inner and outer mitochondria membranes. This event triggers the release of pro-apoptotic proteins, including cytochrome C, from the mitochondrial intermembrane space to the cytosol where they activate caspases and endonucleases that initiates apoptosis. We investigated whether this mechanism occurs in plants as well. Our preliminary results indicate that histone proteins bind to mitochondria and induce mitochondrial membrane permeabilization in plants. We isolated mitochondria and histone fractions from store-bought cauliflower; then a histone-enriched fraction was added to a mitochondria-enriched fraction, incubated, and examined by Western Blotting against histone H3 and cytochrome C. The results show H3 histones in the mitochondrial pellet but not in the supernatant of the experimental sample, cytochrome C in the pellets of the control and experimental sample, and cytochrome C in the supernatant of the experimental sample but not in the control. The results of this study suggest that histone proteins bind to mitochondria affecting the release of cytochrome C from the intermembrane space of the mitochondria and suggest that the interactions between mitochondria and histones may be broadly conserved across eukaryotes.

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Title Annotation:Biological Sciences Paper Abstracts
Publication:Journal of the Alabama Academy of Science
Article Type:Author abstract
Date:Apr 1, 2014
Words:265
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