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Plant Physiol, December 2001, Vol. 127, pp. 1711-1727

Analysis of the Arabidopsis Mitochondrial Proteome1

A. Harvey Millar,* Lee J. Sweetlove, Philippe Giegé, and Christopher J. Leaver

Department of Biochemistry, Faculty of Medicine and Dentistry, and the Plant Sciences Group, Faculty of Agriculture, The University of Western Australia, Crawley 6009, Western Australia, Australia (A.H.M.); and Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom (L.J.S., P.G., C.J.L.)

The complete set of nuclear genes that encode proteins targeted to mitochondria in plants is currently undefined and thus the full range of mitochondrial functions in plants is unknown. Analysis of two-dimensional gel separations of Arabidopsis cell culture mitochondrial protein revealed approximately 100 abundant proteins and 250 low-abundance proteins. Comparison of subfractions of mitochondrial protein on two-dimensional gels provided information on the soluble, membrane, or integral membrane locations of this protein set. A total of 170 protein spots were excised, trypsin-digested, and matrix-assisted laser desorption ionization/time of flight mass spectrometry spectra obtained. Using this dataset, 91 of the proteins were identified by searching translated Arabidopsis genomic databases. Of this set, 81 have defined functions based on sequence comparison. These functions include respiratory electron transport, tricarboxylic acid cycle metabolism, amino acid metabolism, protein import, processing, and assembly, transcription, membrane transport, and antioxidant defense. A total of 10 spectra were matched to Arabidopsis putative open reading frames for which no specific function has been determined. A total of 64 spectra did not match to an identified open reading frame. Analysis of full-length putative protein sequences using bioinformatic tools to predict subcellular targeting (TargetP, Psort, and MitoProt) revealed significant variation in predictions, and also a lack of mitochondrial targeting prediction for several characterized mitochondrial proteins.

1 A.H.M. was supported by an Australian Research Council Australian Postdoctoral Fellowship. This work was also supported by the Biotechnology and Biological Sciences Research Council (to C.J.L.) and by the University of Western Australia Small Grants Scheme (to A.H.M.).

* Corresponding author; e-mail hmillar{at}cyllene.uwa.edu.au; fax 61-8-9380-1148.

© 2001 American Society of Plant Physiologists


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