Structural basis of mitochondrial protein import by the TIM23 complex

Mitochondria import nearly all of their approximately 1,000–2,000 constituent proteins from the cytosol across their double-membrane envelope 1 – 5 . Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing...

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Published in:Nature (London) Vol. 621; no. 7979; pp. 620 - 626
Main Authors: Sim, Sue Im, Chen, Yuanyuan, Lynch, Diane L., Gumbart, James C., Park, Eunyong
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 21.09.2023
Nature Publishing Group
Subjects:
101/28
631/45/535/1258/1259
631/80/2023/2022
631/80/642/333
Amino acids
Cell growth
Cryoelectron Microscopy
Cytosol
Electron microscopy
Humanities and Social Sciences
Imports
Lipids
Membrane proteins
Membranes
Microscopy
Mitochondria
Mitochondria - chemistry
Mitochondria - metabolism
Mitochondria - ultrastructure
Mitochondrial Precursor Protein Import Complex Proteins - chemistry
Mitochondrial Precursor Protein Import Complex Proteins - metabolism
Mitochondrial Precursor Protein Import Complex Proteins - ultrastructure
multidisciplinary
Mutation
Polypeptides
Protein Transport
Proteins
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Science
Science (multidisciplinary)
Substrates
Translocase
Translocation
Yeast
ISSN:0028-0836, 1476-4687, 1476-4687
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Abstract Mitochondria import nearly all of their approximately 1,000–2,000 constituent proteins from the cytosol across their double-membrane envelope 1 – 5 . Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel 6 – 11 . However, the mechanism by which these subunits form a translocation path in the membrane and enable the import process remains unclear due to a lack of structural information. Here we determined the cryo-electron microscopy structure of the core TIM23 complex (heterotrimeric Tim17–Tim23–Tim44) from Saccharomyces cerevisiae . Contrary to the prevailing model, Tim23 and Tim17 themselves do not form a water-filled channel, but instead have separate, lipid-exposed concave cavities that face in opposite directions. Our structural and biochemical analyses show that the cavity of Tim17, but not Tim23, forms the protein translocation path, whereas Tim23 probably has a structural role. The results further suggest that, during translocation of substrate polypeptides, the nonessential subunit Mgr2 seals the lateral opening of the Tim17 cavity to facilitate the translocation process. We propose a new model for the TIM23-mediated protein import and sorting mechanism, a central pathway in mitochondrial biogenesis. The cryo-electron microscopy structure of the mitochondrial TIM23 complex from Saccharomyces cerevisiae shows that Tim17 forms a protein translocation path.
AbstractList Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope1-5. Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel6-11. However, the mechanism by which these subunits form a translocation path in the membrane and enable the import process remains unclear due to a lack of structural information. Here we determined the cryo-electron microscopy structure of the core TIM23 complex (heterotrimeric Tim17-Tim23-Tim44) from Saccharomyces cerevisiae. Contrary to the prevailing model, Tim23 and Tim17 themselves do not form a water-filled channel, but instead have separate, lipid-exposed concave cavities that face in opposite directions. Our structural and biochemical analyses show that the cavity of Tim17, but not Tim23, forms the protein translocation path, whereas Tim23 probably has a structural role. The results further suggest that, during translocation of substrate polypeptides, the nonessential subunit Mgr2 seals the lateral opening of the Tim17 cavity to facilitate the translocation process. We propose a new model for the TIM23-mediated protein import and sorting mechanism, a central pathway in mitochondrial biogenesis.Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope1-5. Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel6-11. However, the mechanism by which these subunits form a translocation path in the membrane and enable the import process remains unclear due to a lack of structural information. Here we determined the cryo-electron microscopy structure of the core TIM23 complex (heterotrimeric Tim17-Tim23-Tim44) from Saccharomyces cerevisiae. Contrary to the prevailing model, Tim23 and Tim17 themselves do not form a water-filled channel, but instead have separate, lipid-exposed concave cavities that face in opposite directions. Our structural and biochemical analyses show that the cavity of Tim17, but not Tim23, forms the protein translocation path, whereas Tim23 probably has a structural role. The results further suggest that, during translocation of substrate polypeptides, the nonessential subunit Mgr2 seals the lateral opening of the Tim17 cavity to facilitate the translocation process. We propose a new model for the TIM23-mediated protein import and sorting mechanism, a central pathway in mitochondrial biogenesis.
Mitochondria import nearly all their ~1,000–2,000 constituent proteins from the cytosol across their double-membrane envelope1–5. Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multi-pass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel6–11. However, the mechanism by which these subunits form a translocation path in the membrane and enable the import process remained unclear due to a lack of structural information. Here, we have determined the cryo-electron microscopy (cryo-EM) structure of the core TIM23 complex (heterotrimeric Tim17–Tim23–Tim44) from Saccharomyces cerevisiae. Contrary to the prevailing model, Tim23 and Tim17 themselves do not form a water-filled channel, but instead have separate, lipid-exposed concave cavities that face in opposite directions. Our structural and biochemical analyses show that surprisingly, the cavity of Tim17, not Tim23, forms the protein translocation path whereas Tim23 is likely to play a structural role. The results further suggest that, during translocation of substrate polypeptides, the nonessential subunit Mgr2 seals the lateral opening of the Tim17 cavity to facilitate the translocation process. We propose a new model for the TIM23-mediated protein import and sorting mechanism, a central pathway in mitochondrial biogenesis.
Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope15. Genetic and biochemical studies have shown that the conserved protein translocase, termed the T1M23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits ofthe T1M23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Timl7, has long been postulated to form a protein-conducting channel6 u. However, the mechanism by which these subunits form a translocation path in the membrane and enable the import process remains unclear due to a lackof structural information. Here we determined the cryo-electron microscopy structure ofthe core T1M23 complex (heterotrimeric Timl7-Tim23-Tim44) from Saccharomyces cerevisiae. Contrarytothe prevailing model, Tim23 and Timl7 themselves do not form a water-filled channel, but instead have separate, lipid-exposed concave cavitiesthat face in opposite directions. Our structural and biochemical analyses showthatthe cavity of Timl7, but not Tim23, forms the protein translocation path, whereas Tim23 probably has a structural role. The results further suggest that, duringtranslocation of substrate polypeptides, the nonessential subunit Mgr2 sealsthe lateral opening ofthe Timl7 cavity to facilitate the translocation process. We propose anew model for the TlM23-mediated protein import and sorting mechanism, a central pathway in mitochondrial biogenesis.
Mitochondria import nearly all of their approximately 1,000–2,000 constituent proteins from the cytosol across their double-membrane envelope 1 – 5 . Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel 6 – 11 . However, the mechanism by which these subunits form a translocation path in the membrane and enable the import process remains unclear due to a lack of structural information. Here we determined the cryo-electron microscopy structure of the core TIM23 complex (heterotrimeric Tim17–Tim23–Tim44) from Saccharomyces cerevisiae . Contrary to the prevailing model, Tim23 and Tim17 themselves do not form a water-filled channel, but instead have separate, lipid-exposed concave cavities that face in opposite directions. Our structural and biochemical analyses show that the cavity of Tim17, but not Tim23, forms the protein translocation path, whereas Tim23 probably has a structural role. The results further suggest that, during translocation of substrate polypeptides, the nonessential subunit Mgr2 seals the lateral opening of the Tim17 cavity to facilitate the translocation process. We propose a new model for the TIM23-mediated protein import and sorting mechanism, a central pathway in mitochondrial biogenesis. The cryo-electron microscopy structure of the mitochondrial TIM23 complex from Saccharomyces cerevisiae shows that Tim17 forms a protein translocation path.
Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope . Genetic and biochemical studies have shown that the conserved protein translocase, termed the TIM23 complex, mediates import of presequence-containing proteins (preproteins) into the mitochondrial matrix and inner membrane. Among about ten different subunits of the TIM23 complex, the essential multipass membrane protein Tim23, together with the evolutionarily related protein Tim17, has long been postulated to form a protein-conducting channel . However, the mechanism by which these subunits form a translocation path in the membrane and enable the import process remains unclear due to a lack of structural information. Here we determined the cryo-electron microscopy structure of the core TIM23 complex (heterotrimeric Tim17-Tim23-Tim44) from Saccharomyces cerevisiae. Contrary to the prevailing model, Tim23 and Tim17 themselves do not form a water-filled channel, but instead have separate, lipid-exposed concave cavities that face in opposite directions. Our structural and biochemical analyses show that the cavity of Tim17, but not Tim23, forms the protein translocation path, whereas Tim23 probably has a structural role. The results further suggest that, during translocation of substrate polypeptides, the nonessential subunit Mgr2 seals the lateral opening of the Tim17 cavity to facilitate the translocation process. We propose a new model for the TIM23-mediated protein import and sorting mechanism, a central pathway in mitochondrial biogenesis.
Author Sim, Sue Im
Chen, Yuanyuan
Gumbart, James C.
Lynch, Diane L.
Park, Eunyong
AuthorAffiliation 3 School of Physics and School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA
1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA
2 California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA
AuthorAffiliation_xml – name: 1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA
– name: 2 California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA
– name: 3 School of Physics and School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, USA
Author_xml – sequence: 1
  givenname: Sue Im
  orcidid: 0000-0003-3560-101X
  surname: Sim
  fullname: Sim, Sue Im
  organization: Department of Molecular and Cell Biology, University of California
– sequence: 2
  givenname: Yuanyuan
  surname: Chen
  fullname: Chen, Yuanyuan
  organization: Department of Molecular and Cell Biology, University of California, California Institute for Quantitative Biosciences, University of California
– sequence: 3
  givenname: Diane L.
  surname: Lynch
  fullname: Lynch, Diane L.
  organization: School of Physics, Georgia Institute of Technology, School of Chemistry and Biochemistry, Georgia Institute of Technology
– sequence: 4
  givenname: James C.
  orcidid: 0000-0002-1510-7842
  surname: Gumbart
  fullname: Gumbart, James C.
  organization: School of Physics, Georgia Institute of Technology, School of Chemistry and Biochemistry, Georgia Institute of Technology
– sequence: 5
  givenname: Eunyong
  orcidid: 0000-0003-2994-5174
  surname: Park
  fullname: Park, Eunyong
  email: eunyong_park@berkeley.edu
  organization: Department of Molecular and Cell Biology, University of California, California Institute for Quantitative Biosciences, University of California
BackLink https://www.ncbi.nlm.nih.gov/pubmed/37344598$$D View this record in MEDLINE/PubMed
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E.P. conceived and supervised the project; S.I.S. constructed yeast strains and prepared samples for cryo-EM analysis; S.I.S. and E.P. developed anti-Tim44 antibodies, collected and analyzed cryo-EM data, and built atomic models; Y.C. performed mutational analysis; Y.C. and S.I.S. performed biochemical experiments; D.L. and J.C.G. performed MD simulations; E.P. wrote the manuscript with input from all authors; all authors contributed to data interpretations and manuscript editing.
These authors contributed equally to this work.
Authors contributions
ORCID 0000-0003-3560-101X
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Snippet Mitochondria import nearly all of their approximately 1,000–2,000 constituent proteins from the cytosol across their double-membrane envelope 1 – 5 . Genetic...
Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope . Genetic and...
Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope15. Genetic and...
Mitochondria import nearly all of their approximately 1,000-2,000 constituent proteins from the cytosol across their double-membrane envelope1-5. Genetic and...
Mitochondria import nearly all their ~1,000–2,000 constituent proteins from the cytosol across their double-membrane envelope1–5. Genetic and biochemical...
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SubjectTerms 101/28
631/45/535/1258/1259
631/80/2023/2022
631/80/642/333
Amino acids
Cell growth
Cryoelectron Microscopy
Cytosol
Electron microscopy
Humanities and Social Sciences
Imports
Lipids
Membrane proteins
Membranes
Microscopy
Mitochondria
Mitochondria - chemistry
Mitochondria - metabolism
Mitochondria - ultrastructure
Mitochondrial Precursor Protein Import Complex Proteins - chemistry
Mitochondrial Precursor Protein Import Complex Proteins - metabolism
Mitochondrial Precursor Protein Import Complex Proteins - ultrastructure
multidisciplinary
Mutation
Polypeptides
Protein Transport
Proteins
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Science
Science (multidisciplinary)
Substrates
Translocase
Translocation
Yeast
Title Structural basis of mitochondrial protein import by the TIM23 complex
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