Structure of the F-actin–tropomyosin complex

Electron cryomicroscopy reveals the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å; the stabilizing interactions and the effects of disease-causing mutants are also investigated. The interaction of F-actin and tropomyosin (Rausner...

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Published inNature (London) Vol. 519; no. 7541; pp. 114 - 117
Main Authors von der Ecken, Julian, Müller, Mirco, Lehman, William, Manstein, Dietmar J., Penczek, Pawel A., Raunser, Stefan
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 05.03.2015
Nature Publishing Group
Subjects
101/28
631/535/1258/1259
631/80/128/1276
Actin
Actins - chemistry
Actins - genetics
Actins - metabolism
Adenosine Diphosphate - metabolism
Analysis
Animals
Cryoelectron Microscopy
Cytoskeleton
Genetic aspects
Hearing loss
Humanities and Social Sciences
letter
Magnesium - metabolism
Mice
Models, Molecular
Molecular structure
multidisciplinary
Muscle proteins
Mutation
Mutation - genetics
Myosin
Polymerization
Protein Conformation
Proteins
Rabbits
Science
Static Electricity
Tropomyosin - chemistry
Tropomyosin - genetics
Tropomyosin - metabolism
United States
Online AccessGet full text

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Abstract Electron cryomicroscopy reveals the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å; the stabilizing interactions and the effects of disease-causing mutants are also investigated. The interaction of F-actin and tropomyosin (Rausner SS) Filamentous actin (F-actin) — a main component of the cytoskeleton — is the major protein of thin filaments in the muscle. The binding of the motor protein myosin to F-actin is mediated by another protein called tropomyosin, which also binds to F-actin in smooth muscle and in non-muscle cells, stabilizing and regulating these filaments. Using electron cryomicroscopy, Stefan Raunser and colleagues have obtained the first high-resolution, three-dimensional structure of F-actin in complex with tropomyosin. The structure reveals the interactions that stabilize the F-actin and sheds light on the possible effect of prominent disease-causing mutations. Comparison of the F-actin structure with the crystal structure of monomeric (G)-actin reveals conformational changes associated with filament formation. Filamentous actin (F-actin) is the major protein of muscle thin filaments, and actin microfilaments are the main component of the eukaryotic cytoskeleton. Mutations in different actin isoforms lead to early-onset autosomal dominant non-syndromic hearing loss 1 , familial thoracic aortic aneurysms and dissections 2 , and multiple variations of myopathies 3 . In striated muscle fibres, the binding of myosin motors to actin filaments is mainly regulated by tropomyosin and troponin 4 , 5 . Tropomyosin also binds to F-actin in smooth muscle and in non-muscle cells and stabilizes and regulates the filaments there in the absence of troponin 6 . Although crystal structures for monomeric actin (G-actin) are available 7 , a high-resolution structure of F-actin is still missing, hampering our understanding of how disease-causing mutations affect the function of thin muscle filaments and microfilaments. Here we report the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å, determined by electron cryomicroscopy. The structure reveals that the D-loop is ordered and acts as a central region for hydrophobic and electrostatic interactions that stabilize the F-actin filament. We clearly identify map density corresponding to ADP and Mg 2+ and explain the possible effect of prominent disease-causing mutants. A comparison of F-actin with G-actin reveals the conformational changes during filament formation and identifies the D-loop as their key mediator. We also confirm that negatively charged tropomyosin interacts with a positively charged groove on F-actin. Comparison of the position of tropomyosin in F-actin–tropomyosin with its position in our previously determined F-actin–tropomyosin–myosin structure 8 reveals a myosin-induced transition of tropomyosin. Our results allow us to understand the role of individual mutations in the genesis of actin- and tropomyosin-related diseases and will serve as a strong foundation for the targeted development of drugs.
AbstractList Filamentous actin (F-actin) is the major protein of muscle thin filaments, and actin microfilaments are the main component of the eukaryotic cytoskeleton. Mutations in different actin isoforms lead to early-onset autosomal dominant non-syndromic hearing loss^sup 1^, familial thoracic aortic aneurysms and dissections^sup 2^, and multiple variations of myopathies^sup 3^. In striated muscle fibres, the binding of myosin motors to actin filaments is mainly regulated by tropomyosin and troponin^sup 4,5^. Tropomyosin also binds to F-actin in smooth muscle and in non-muscle cells and stabilizes and regulates the filaments there in the absence of troponin^sup 6^. Although crystal structures for monomericactin (G-actin) are available^sup 7^, a high-resolution structure of F-actin is still missing, hampering our understanding of how disease-causing mutations affect the function of thin muscle filaments and microfilaments. Here we report the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5Å, determined by electron cryomicroscopy. The structure reveals that the D-loop is ordered and acts as a central region for hydrophobic and electrostatic interactions that stabilize the F-actin filament. We clearly identify map density corresponding to ADP and Mg^sup 2+^ and explain the possible effect of prominent disease-causing mutants. A comparison of F-actin with G-actin reveals the conformational changes during filament formation and identifies the D-loop as their key mediator. We also confirm that negatively charged tropomyosin interacts with a positively charged groove on F-actin. Comparison of the position of tropomyosin in F-actin-tropomyosin with its position in our previously determined F-actin-tropomyosin-myosin structure^sup 8^ reveals a myosin-induced transition of tropomyosin. Our results allow us to understand the role of individual mutations in the genesis of actin-and tropomyosin-related diseases and will serve as a strong foundation for the targeted development of drugs.
Filamentous actin (F-actin) is the major protein of muscle thin filaments, and actin microfilaments are the main component of the eukaryotic cytoskeleton. Mutations in different actin isoforms lead to early-onset autosomal dominant non-syndromic hearing loss, familial thoracic aortic aneurysms and dissections, and multiple variations of myopathies. In striated muscle fibres, the binding of myosin motors to actin filaments is mainly regulated by tropomyosin and troponin. Tropomyosin also binds to F-actin in smooth muscle and in non-muscle cells and stabilizes and regulates the filaments there in the absence of troponin. Although crystal structures for monomeric actin (G-actin) are available, a high-resolution structure of F-actin is still missing, hampering our understanding of how disease-causing mutations affect the function of thin muscle filaments and microfilaments. Here we report the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å, determined by electron cryomicroscopy. The structure reveals that the D-loop is ordered and acts as a central region for hydrophobic and electrostatic interactions that stabilize the F-actin filament. We clearly identify map density corresponding to ADP and Mg(2+) and explain the possible effect of prominent disease-causing mutants. A comparison of F-actin with G-actin reveals the conformational changes during filament formation and identifies the D-loop as their key mediator. We also confirm that negatively charged tropomyosin interacts with a positively charged groove on F-actin. Comparison of the position of tropomyosin in F-actin-tropomyosin with its position in our previously determined F-actin-tropomyosin-myosin structure reveals a myosin-induced transition of tropomyosin. Our results allow us to understand the role of individual mutations in the genesis of actin- and tropomyosin-related diseases and will serve as a strong foundation for the targeted development of drugs.
Filamentous actin (F-actin) is the major protein of muscle thin filaments, and actin microfilaments are the main component of the eukaryotic cytoskeleton. Mutations in different actin isoforms lead to early-onset autosomal dominant non-syndromic hearing loss 1 , familial thoracic aortic aneurysms and dissections 2 , and multiple variations of myopathies 3 . In striated muscle fibres, the binding of myosin motors to actin filaments is mainly regulated by tropomyosin and troponin 4 , 5 . Tropomyosin also binds to F-actin in smooth muscle and in non-muscle cells and stabilizes and regulates the filaments there in the absence of troponin 6 . Although crystal structures for monomeric actin (G-actin) are available 7 , a high-resolution structure of F-actin is still missing, hampering our understanding of how disease-causing mutations affect the function of thin muscle filaments and microfilaments. Here we report the three-dimensional structure of F-actin at a resolution of 3.7 ångstroms in complex with tropomyosin at a resolution of 6.5ångstroms, determined by electron cryomicroscopy. The structure reveals that the D-loop is ordered and acts as a central region for hydrophobic and electrostatic interactions that stabilize the F-actin filament. We clearly identify the density corresponding to ADP and Mg 2+ and explain the possible effect of prominent disease-causing mutants. A comparison of F-actin with G-actin reveals the conformational changes during filament formation and identifies the D-loop as their key mediator. We also confirm that negatively charged tropomyosin interacts with a positively charged groove on F-actin. Comparison of the position of tropomyosin in F-actin–tropomyosin with its position in our previously determined actin–tropomyosin–myosin structure 8 reveals a myosin-induced transition of tropomyosin. Our results allow us to understand the role of individual mutations in the genesis of actin- and tropomyosin-related diseases and will serve as a strong foundation for the targeted development of drugs.
Electron cryomicroscopy reveals the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å; the stabilizing interactions and the effects of disease-causing mutants are also investigated. The interaction of F-actin and tropomyosin (Rausner SS) Filamentous actin (F-actin) — a main component of the cytoskeleton — is the major protein of thin filaments in the muscle. The binding of the motor protein myosin to F-actin is mediated by another protein called tropomyosin, which also binds to F-actin in smooth muscle and in non-muscle cells, stabilizing and regulating these filaments. Using electron cryomicroscopy, Stefan Raunser and colleagues have obtained the first high-resolution, three-dimensional structure of F-actin in complex with tropomyosin. The structure reveals the interactions that stabilize the F-actin and sheds light on the possible effect of prominent disease-causing mutations. Comparison of the F-actin structure with the crystal structure of monomeric (G)-actin reveals conformational changes associated with filament formation. Filamentous actin (F-actin) is the major protein of muscle thin filaments, and actin microfilaments are the main component of the eukaryotic cytoskeleton. Mutations in different actin isoforms lead to early-onset autosomal dominant non-syndromic hearing loss 1 , familial thoracic aortic aneurysms and dissections 2 , and multiple variations of myopathies 3 . In striated muscle fibres, the binding of myosin motors to actin filaments is mainly regulated by tropomyosin and troponin 4 , 5 . Tropomyosin also binds to F-actin in smooth muscle and in non-muscle cells and stabilizes and regulates the filaments there in the absence of troponin 6 . Although crystal structures for monomeric actin (G-actin) are available 7 , a high-resolution structure of F-actin is still missing, hampering our understanding of how disease-causing mutations affect the function of thin muscle filaments and microfilaments. Here we report the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å, determined by electron cryomicroscopy. The structure reveals that the D-loop is ordered and acts as a central region for hydrophobic and electrostatic interactions that stabilize the F-actin filament. We clearly identify map density corresponding to ADP and Mg 2+ and explain the possible effect of prominent disease-causing mutants. A comparison of F-actin with G-actin reveals the conformational changes during filament formation and identifies the D-loop as their key mediator. We also confirm that negatively charged tropomyosin interacts with a positively charged groove on F-actin. Comparison of the position of tropomyosin in F-actin–tropomyosin with its position in our previously determined F-actin–tropomyosin–myosin structure 8 reveals a myosin-induced transition of tropomyosin. Our results allow us to understand the role of individual mutations in the genesis of actin- and tropomyosin-related diseases and will serve as a strong foundation for the targeted development of drugs.
Audience Academic
Author Müller, Mirco
Manstein, Dietmar J.
von der Ecken, Julian
Lehman, William
Raunser, Stefan
Penczek, Pawel A.
AuthorAffiliation 2 Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany
3 Department of Physiology and Biophysics, Boston University School of Medicine, 72 East Concord Street, Boston, Massachusetts 02118, USA
4 Department of Biochemistry and Molecular Biology, The University of Texas, Houston Medical School, Houston, Texas 77030, USA
1 Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
AuthorAffiliation_xml – name: 3 Department of Physiology and Biophysics, Boston University School of Medicine, 72 East Concord Street, Boston, Massachusetts 02118, USA
– name: 2 Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany
– name: 4 Department of Biochemistry and Molecular Biology, The University of Texas, Houston Medical School, Houston, Texas 77030, USA
– name: 1 Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
Author_xml – sequence: 1
  givenname: Julian
  surname: von der Ecken
  fullname: von der Ecken, Julian
  organization: Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
– sequence: 2
  givenname: Mirco
  surname: Müller
  fullname: Müller, Mirco
  organization: Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany
– sequence: 3
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  surname: Lehman
  fullname: Lehman, William
  organization: Department of Physiology and Biophysics, Boston University School of Medicine
– sequence: 4
  givenname: Dietmar J.
  surname: Manstein
  fullname: Manstein, Dietmar J.
  organization: Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany
– sequence: 5
  givenname: Pawel A.
  surname: Penczek
  fullname: Penczek, Pawel A.
  organization: Department of Biochemistry and Molecular Biology, The University of Texas, Houston Medical School
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  givenname: Stefan
  surname: Raunser
  fullname: Raunser, Stefan
  email: stefan.raunser@mpi-dortmund.mpg.de
  organization: Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
BackLink https://www.ncbi.nlm.nih.gov/pubmed/25470062$$D View this record in MEDLINE/PubMed
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Snippet Electron cryomicroscopy reveals the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å; the...
Filamentous actin (F-actin) is the major protein of muscle thin filaments, and actin microfilaments are the main component of the eukaryotic cytoskeleton....
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StartPage 114
SubjectTerms 101/28
631/535/1258/1259
631/80/128/1276
Actin
Actins - chemistry
Actins - genetics
Actins - metabolism
Adenosine Diphosphate - metabolism
Analysis
Animals
Cryoelectron Microscopy
Cytoskeleton
Genetic aspects
Hearing loss
Humanities and Social Sciences
letter
Magnesium - metabolism
Mice
Models, Molecular
Molecular structure
multidisciplinary
Muscle proteins
Mutation
Mutation - genetics
Myosin
Polymerization
Protein Conformation
Proteins
Rabbits
Science
Static Electricity
Tropomyosin - chemistry
Tropomyosin - genetics
Tropomyosin - metabolism
Title Structure of the F-actin–tropomyosin complex
URI https://link.springer.com/article/10.1038/nature14033
https://www.ncbi.nlm.nih.gov/pubmed/25470062
https://www.proquest.com/docview/1662769895
https://search.proquest.com/docview/1661327342
https://pubmed.ncbi.nlm.nih.gov/PMC4477711
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