Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules.

Molecular and Cellular Biology
K R RyanRobert E Jensen

Abstract

Tim23p is a mitochondrial inner membrane protein essential for the import of proteins from the cytosol. Tim23p contains an amino-terminal hydrophilic segment and a carboxyl-terminal hydrophobic domain (Tim23Cp). To study the functions and interactions of the two parts of Tim23p separately, we constructed tim23N, encoding only the hydrophilic region of Tim23p, and tim23C, encoding only the hydrophobic domain of Tim23p. Only the Tim23C protein is imported into mitochondria, indicating that the mitochondrial targeting information in Tim23p resides in its membrane spans or intervening loops. Tim23Cp, however, cannot substitute for full-length Tim23p, suggesting that the hydrophilic portion of Tim23p also performs an essential function in mitochondrial protein import. We found that overexpression of Tim23Cp is toxic to yeast cells that carry the tim23-1 mutation. Excess Tim23Cp causes Tim23-1p to disappear, leaving tim23-1 cells without a full-length version of the Tim23 protein. If Tim17p, another inner membrane import component, is overexpressed along with Tim23Cp, the toxicity of Tim23Cp is largely reversed and the Tim23-1 protein no longer disappears. In coimmunoprecipitations from solubilized mitochondria, Tim17p associates wit...Continue Reading

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Citations

Feb 2, 2010·Biochimica Et Biophysica Acta·Dejana Mokranjac, Walter Neupert
Apr 18, 2003·Current Biology : CB·Kaye N TruscottNikolaus Pfanner
Aug 23, 2002·Biochimica Et Biophysica Acta·Nikolaus Pfanner, Agnieszka Chacinska
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Nov 4, 2005·Molecular Biology of the Cell·Cory D DunnRobert E Jensen
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Jul 29, 2003·The Journal of Biological Chemistry·Scott AllenKostas Tokatlidis
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