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Originally published In Press as doi:10.1074/mcp.M700490-MCP200 on March 24, 2008.
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Molecular & Cellular Proteomics 7:1286-1296, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Trypanosoma brucei Mitochondrial Ribosomes

Affinity Purification and Component Identification by Mass Spectrometry*,S

Alena Zíková, Aswini K. Panigrahi, Rachel A. Dalley, Nathalie Acestor, Atashi Anupama, Yuko Ogata, Peter J. Myler and Kenneth Stuart{ddagger}

From the Seattle Biomedical Research Institute, Seattle, Washington 98109

Although eukaryotic mitochondrial (mt) ribosomes evolved from a putative prokaryotic ancestor their compositions vary considerably among organisms. We determined the protein composition of tandem affinity-purified Trypanosoma brucei mt ribosomes by mass spectrometry and identified 133 proteins of which 77 were associated with the large subunit and 56 were associated with the small subunit. Comparisons with bacterial and mammalian mt ribosomal proteins identified T. brucei mt homologs of L2–4, L7/12, L9, L11, L13–17, L20–24, L27–30, L33, L38, L43, L46, L47, L49, L52, S5, S6, S8, S9, S11, S15–18, S29, and S34, although the degree of conservation varied widely. Sequence characteristics of some of the component proteins indicated apparent functions in rRNA modification and processing, protein assembly, and mitochondrial metabolism implying possible additional roles for these proteins. Nevertheless most of the identified proteins have no homology outside Kinetoplastida implying very low conservation and/or a divergent function in kinetoplastid mitochondria.

{ddagger} To whom correspondence should be addressed: Seattle Biomedical Research Inst., 307 Westlake Ave. N., Suite 500, Seattle, WA 98109-5219. Tel.: 206-256-7316; Fax: 206-256-7229; E-mail: ken.stuart{at}sbri.org


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