TY - JOUR
T1 - Functions of outer membrane receptors in mitochondrial protein import
AU - Endo, Toshiya
AU - Kohda, Daisuke
N1 - Funding Information:
Our own work cited here was supported by Grants in aid for Scientific Research from the Ministry of Education, Science and Culture of Japan. We thank Toshihiro Shodai, Shuh-ichi Nishikawa, Tohru Yoshihisa, Yoshito Abe, Takanori Muto, Takayuki Obita, and Katsuyoshi Mihara as well as our collaborators for helpful comments and discussions.
PY - 2002/9/2
Y1 - 2002/9/2
N2 - Most mitochondrial proteins are synthesized in the cytosol as precursor proteins and are imported into mitochondria. The targeting signals for mitochondria are encoded in the presequences or in the mature parts of the precursor proteins, and are decoded by the receptor sites in the translocator complex in the mitochondrial outer membrane. The recently determined NMR structure of the general import receptor Tom20 in a complex with a presequence peptide reveals that, although the amphiphilicity and positive charges of the presequence is essential for the import ability of the presequence, Tom20 recognizes only the amphiphilicity, but not the positive charges. This leads to a new model that different features associated with the mitochondrial targeting sequence of the precursor protein can be recognized by the mitochondrial protein import system in different steps during the import.
AB - Most mitochondrial proteins are synthesized in the cytosol as precursor proteins and are imported into mitochondria. The targeting signals for mitochondria are encoded in the presequences or in the mature parts of the precursor proteins, and are decoded by the receptor sites in the translocator complex in the mitochondrial outer membrane. The recently determined NMR structure of the general import receptor Tom20 in a complex with a presequence peptide reveals that, although the amphiphilicity and positive charges of the presequence is essential for the import ability of the presequence, Tom20 recognizes only the amphiphilicity, but not the positive charges. This leads to a new model that different features associated with the mitochondrial targeting sequence of the precursor protein can be recognized by the mitochondrial protein import system in different steps during the import.
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U2 - 10.1016/S0167-4889(02)00259-8
DO - 10.1016/S0167-4889(02)00259-8
M3 - Review article
C2 - 12191763
AN - SCOPUS:0037009087
SN - 0167-4889
VL - 1592
SP - 3
EP - 14
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
IS - 1
ER -