Ontology highlight
ABSTRACT:
SUBMITTER: Yamamoto H
PROVIDER: S-EPMC3017135 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Yamamoto Hayashi H Itoh Nobuka N Kawano Shin S Yatsukawa Yoh-ichi Y Momose Takaki T Makio Tadashi T Matsunaga Mayumi M Yokota Mihoko M Esaki Masatoshi M Shodai Toshihiro T Kohda Daisuke D Hobbs Alyson E Aiken AE Jensen Robert E RE Endo Toshiya T
Proceedings of the National Academy of Sciences of the United States of America 20101220 1
Mitochondria import most of their resident proteins from the cytosol, and the import receptor Tom20 of the outer-membrane translocator TOM40 complex plays an essential role in specificity of mitochondrial protein import. Here we analyzed the effects of Tom20 binding on NMR spectra of a long mitochondrial presequence and found that it contains two distinct Tom20-binding elements. In vitro import and cross-linking experiments revealed that, although the N-terminal Tom20-binding element is essentia ...[more]