Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria
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 mitochon...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 108; no. 1; pp. 91 - 96 |
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| Main Authors | , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
04.01.2011
National Acad Sciences |
| Subjects | |
| Online Access | Get full text |
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| Abstract | 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 essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in the step prior to translocation across the inner membrane. Therefore Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency. |
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| AbstractList | 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 essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in the step prior to translocation across the inner membrane. Therefore Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency. 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 essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in the step prior to translocation across the inner membrane. Therefore Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency. [PUBLICATION ABSTRACT] 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 essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in the step prior to translocation across the inner membrane. Therefore Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency.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 essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in the step prior to translocation across the inner membrane. Therefore Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency. |
| Author | Momose, Takaki Yokota, Mihoko Kohda, Daisuke Esaki, Masatoshi Aiken Hobbs, Alyson E Endo, Toshiya Itoh, Nobuka Makio, Tadashi Yatsukawa, Yoh-ichi Kawano, Shin Jensen, Robert E Matsunaga, Mayumi Yamamoto, Hayashi Shodai, Toshihiro |
| Author_xml | – sequence: 1 fullname: Yamamoto, Hayashi – sequence: 2 fullname: Itoh, Nobuka – sequence: 3 fullname: Kawano, Shin – sequence: 4 fullname: Yatsukawa, Yoh-ichi – sequence: 5 fullname: Momose, Takaki – sequence: 6 fullname: Makio, Tadashi – sequence: 7 fullname: Matsunaga, Mayumi – sequence: 8 fullname: Yokota, Mihoko – sequence: 9 fullname: Esaki, Masatoshi – sequence: 10 fullname: Shodai, Toshihiro – sequence: 11 fullname: Kohda, Daisuke – sequence: 12 fullname: Aiken Hobbs, Alyson E – sequence: 13 fullname: Jensen, Robert E – sequence: 14 fullname: Endo, Toshiya |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21173275$$D View this record in MEDLINE/PubMed |
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| Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 2Present address: Frontier Research Center, Tokyo Institute of Technology, Nagatsuta-cho 4259-S2, Midori-ku, Yokohama 226-8503, Japan. 3Present address: Department of Cell Biology, University of Alberta, Edmonton, AB, Canada T6G 2H7. 4Present address: Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811, Japan. Author contributions: H.Y., N.I., S.K., M.E., and T.E. designed research; H.Y., N.I., S.K., Y.Y., T. Momose, T. Makio, M.M., M.Y., and T.S. performed research; H.Y., N.I., S.K., Y.Y., T. Momose, T. Makio, M.M., M.Y., and D.K. analyzed data; A.E.A.H. and R.E.J. contributed new reagents/analytic tools; and H.Y., N.I., S.K., and T.E. wrote the paper. 1H.Y. and N.I. contributed equally to this work. Edited by Walter Neupert, University of Munich, Munich, Germany, and accepted by the Editorial Board November 13, 2010 (received for review October 5, 2010) |
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| SubjectTerms | Amino acids Binding sites Binding Sites - genetics Biological Sciences crosslinking cytosol Immunoprecipitation Imports in vitro studies Membranes Mitochondria Mitochondria - metabolism Mitochondrial Membrane Transport Proteins - metabolism Models, Molecular nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance, Biomolecular P branes Protein Binding - genetics Protein Binding - physiology Protein precursors Protein transport Protein Transport - physiology Proteins Proton-Translocating ATPases - genetics Proton-Translocating ATPases - metabolism Receptors Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - metabolism T cell receptors Translocation Yeasts |
| Title | Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria |
| URI | https://www.jstor.org/stable/25770732 http://www.pnas.org/content/108/1/91.abstract https://www.ncbi.nlm.nih.gov/pubmed/21173275 https://www.proquest.com/docview/822924315 https://www.proquest.com/docview/1817810272 https://www.proquest.com/docview/822710226 https://pubmed.ncbi.nlm.nih.gov/PMC3017135 |
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