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Originally published as MBC in Press, 10.1091/mbc.E07-07-0669 on October 24, 2007

Vol. 19, Issue 1, 159-170, January 2008

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Quaternary Structure of the Mitochondrial TIM23 Complex Reveals Dynamic Association between Tim23p and Other Subunits

Nathan N. Alder*, Jennifer Sutherland*, Ashley I. Buhring*, Robert E. Jensen{dagger}, and Arthur E. Johnson*,{ddagger}

*Department of Molecular and Cellular Medicine and {ddagger}Departments of Chemistry and of Biochemistry and Biophysics, Texas A&M University System Health Science Center, College Station, TX 77843-1114; and {dagger}Department of Cell Biology and Anatomy, Johns Hopkins School of Medicine, Baltimore, MD 21205

Submitted July 16, 2007; Revised September 27, 2007; Accepted October 17, 2007
Monitoring Editor: Reid Gilmore

Tim23p is an essential channel-forming component of the multisubunit TIM23 complex of the mitochondrial inner membrane that mediates protein import. Radiolabeled Tim23p monocysteine mutants were imported in vitro, incorporated into functional TIM23 complexes, and subjected to chemical cross-linking. Three regions of proximity between Tim23p and other subunits of the TIM23 complex were identified: Tim17p and the first transmembrane segment of Tim23p; Tim50p and the C-terminal end of the Tim23p hydrophilic region; and the entire hydrophilic domains of Tim23p molecules. These regions of proximity reversibly change in response to changes in membrane potential across the inner membrane and also when a translocating substrate is trapped in the TIM23 complex. These structural changes reveal that the macromolecular arrangement within the TIM23 complex is dynamic and varies with the physiological state of the mitochondrion.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-07-0669) on October 24, 2007.

Address correspondence to: Arthur E. Johnson (ajohnson{at}medicine.tamhsc.edu)






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