Proteomic analysis of mitochondria from Caenorhabditis elegans |
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Authors: | Jing Li Tanxi Cai Peng Wu Ziyou Cui Xiulan Chen Junjie Hou Zhensheng Xie Peng Xue Linan Shi Pingsheng Liu John R. Yates III Fuquan Yang |
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Affiliation: | 1. Proteomic Platform, Institute of Biophysics, Chinese Academy of Sciences, Beijing, P. R. China;2. Graduate University of the Chinese Academy of Sciences, Beijing, P. R. China;3. Center for Structure Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing, P. R. China;4. Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, USA |
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Abstract: | Mitochondria play essential roles in cell physiological processes including energy production, metabolism, ion homeostasis, cell growth, aging and apoptosis. Proteomic strategies have been applied to the study of mitochondria since 1998; these studies have yielded decisive information about the diverse physiological functions of the organelle. As an ideal model biological system, the nematode Caenorhabditis elegans has been widely used in the study of several diseases, such as metabolic diseases and cancer. However, the mitochondrial proteome of C. elegans remains elusive. In this study, we purified mitochondria from C. elegans and performed a comprehensive proteomic analysis using the shotgun proteomic approach. A total of 1117 proteins have been identified with at least two unique peptides. Their physicochemical and functional characteristics, subcellular locations, related biological processes, and associations with human diseases, especially Parkinson's disease, are discussed. An orthology comparison was also performed between C. elegans and four other model organisms for a general depiction of the conservation of mitochondrial proteins during evolution. This study will provide new clues for understanding the role of mitochondria in the physiological and pathological processes of C. elegans. |
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Keywords: | Animal proteomics Caenorhabditis elegans Development Evolutionary conservation Mitochondrial proteomics Shotgun proteomics |
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