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A more recent version of this article appeared on June 1, 2004
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Submitted on February 12, 2004
Revised on March 12, 2004
Accepted on March 12, 2004
1 Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, AZ 85721; Present address: Botanisches Institut der Christian-Albrechts-Universität zu Kiel, Am Botanischen Garten 1-9, D-24118 Kiel, Germany
2 Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, AZ 85721
3 Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, AZ 85721; Present address: Bioreliance Inc., 5 Biotech, 381 Plantation Street, Worcester, MA 01605
* Corresponding author. E-mail address: dieckman{at}email.arizona.edu.
In S. cerevisiae, the nuclear-encoded protein Cbp1 promotes stability and translation of mitochondrial cytochrome b (COB) transcripts through interaction with the 5' UTR. Fusion of a biotin-binding peptide tag to the C-terminus of Cbp1 has now allowed detection in mitochondrial extracts using peroxidase-coupled avidin. Cbp1 is associated with the mitochondrial membranes when high ionic strength extraction conditions are used. However, the protein is easily solubilized by omitting salt from the extraction buffer, which suggests Cbp1 is loosely associated with the membrane through weak hydrophobic interactions. Gel filtration analysis and blue native PAGE showed that Cbp1 is part of a single, 900,000 dalton complex. The complex was purified utilizing the biotin tag and a sequence-specific protease cleavage site. In addition to Cbp1, the complex contains several polypeptides of molecular weights between 113 and 40 kDa. Among these we identified another message-specific factor, Pet309, which promotes the stability and translation of mitochondrial cytochrome oxidase subunit I (COX1) mRNA. A hypothesis is presented in which the Cbp1-Pet309 complex contains several message-specific RNA binding proteins and links transcription to translation of the mRNAs at the membrane.
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