TY - JOUR
T1 - Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
AU - Abe, Yoshito
AU - Shodai, Toshihiro
AU - Muto, Takanori
AU - Mihara, Katsuyoshi
AU - Torii, Hisayoshi
AU - Nishikawa, Shuh ichi
AU - Endo, Toshiya
AU - Kohda, Daisuke
N1 - Funding Information:
We thank Drs. T. Tanaka and Y. Tanaka for peptide synthesis, Drs. T. Mizukoshi and S. Kurihara for the synthesis of N-Fmoc-[ 2 H]leucine, Dr. H. Nakamura for the program EMBOSS, and Drs. A. Bocquier, K. Morikawa, and N. Pfanner for critical reading of the manuscript. This project was supported by Grants-in-aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, and by a grant for the Biodesign Research Program from the Institute of Physical and Chemical Research (T. E.).
PY - 2000/3/3
Y1 - 2000/3/3
N2 - Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with a cleavable N-terminal presequence and are imported into mitochondria. We report here the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all α-helical structure with a groove to accommodate the presequence peptide. The bound presequence forms an amphiphilic helical structure with hydrophobic leucines aligned on one side to interact with a hydrophobic patch in the Tom20 groove. Although the positive charges of the presequence are essential for import ability, presequence binding to Tom20 is mediated mainly by hydrophobic rather than ionic interactions.
AB - Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with a cleavable N-terminal presequence and are imported into mitochondria. We report here the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all α-helical structure with a groove to accommodate the presequence peptide. The bound presequence forms an amphiphilic helical structure with hydrophobic leucines aligned on one side to interact with a hydrophobic patch in the Tom20 groove. Although the positive charges of the presequence are essential for import ability, presequence binding to Tom20 is mediated mainly by hydrophobic rather than ionic interactions.
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U2 - 10.1016/S0092-8674(00)80691-1
DO - 10.1016/S0092-8674(00)80691-1
M3 - Article
C2 - 10721992
AN - SCOPUS:0034598904
SN - 0092-8674
VL - 100
SP - 551
EP - 560
JO - Cell
JF - Cell
IS - 5
ER -