TY  - JOUR
AU  - Beddoe, T
AU  - Bushell, SR
AU  - Perugini, MA
AU  - Lithgow, T
AU  - Mulhern, TD
AU  - Bottomley, SP
AU  - Rossjohn, J
Y2  - 2014/05/21
Y1  - 2004/11/05
SN  - 0021-9258
UR  - http://hdl.handle.net/11343/26576
AB  - Proteins destined for all submitochondrial compartments are translocated across the outer mitochondrial membrane by the TOM (translocase of the outer membrane) complex, which consists of a number of specialized receptor subunits that bind mitochondrial precursor proteins for delivery into the translocation channel. One receptor, Tom70, binds large, hydrophobic mitochondrial precursors. The current model of Tom70-mediated import involves multiple dimers of the receptor recognizing a single molecule of substrate. Here we show via a battery of biophysical and spectroscopic techniques that the cytosolic domain of Tom70 is an elongated monomer. Thermal and urea-induced denaturation revealed that the receptor, which unfolds via a multistate pathway, is a relatively unstable molecule undergoing major conformational change at physiological temperatures. The data suggest that the malleability of the monomeric Tom70 receptor is an important factor in mitochondrial import.
N1  - application/pdf
LA  - English
PB  - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
KW  - Biochemistry and Cell Biology not elsewhere classified ; Biological Sciences
T1  - A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway
DO  - 10.1074/jbc.M405639200
IS  - Journal of Biological Chemistry
VL  - 279
IS  - 45
SP  - 46448-46454
L1  - /bitstream/handle/11343/26576/116380_5427.pdf?sequence=1&isAllowed=n
ER  -