Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12

The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 μm) depends on its midline α-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human S...

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Published inNature structural & molecular biology Vol. 28; no. 8; pp. 681 - 693
Main Authors Dunce, James M., Salmon, Lucy J., Davies, Owen R.
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.08.2021
Nature Publishing Group
Subjects
101/28
631/45/612/100/101
631/45/612/1228
631/535/1258
631/535/1261
631/535/1266
82/29
82/80
82/83
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Biophysics
Cell Cycle Proteins - metabolism
Cell research
Cellular proteins
Chromosome Pairing - physiology
Chromosomes
Coils
Crystal structure
Crystallography
Crystallography, X-Ray
Cytoskeletal Proteins - metabolism
Cytoskeleton
Electron microscopy
Elongated structure
Elongation
Fibers
Homology
Humans
Keratin
Keratins - metabolism
Lamins - metabolism
Life Sciences
Long fibers
Meiosis
Meiosis - physiology
Membrane Biology
Microscopy
Mutagenesis
Oligomers
Protein Structure
Protein Structure, Quaternary
Proteins
Self-assembly
Structure
Synaptonemal complex
Synaptonemal Complex - metabolism
Vimentin
Vimentin - metabolism
United Kingdom
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Abstract The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 μm) depends on its midline α-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building block and on assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fiber assembly. SYCE2-TEX12’s building blocks are 2:2 coiled coils that dimerize into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibers that intertwine within 40-nm bundled micrometer-long fibers that define the SC’s midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behavior typical of cytoskeletal proteins to provide an α-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes. Crystallographic, electron microscopy and biophysical studies reveal how the synaptonemal complex component SYCE2-TEX12 undergoes self-assembly into fibrous supramolecular structures that mediate homologous chromosome synapsis in meiosis.
AbstractList The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 μm) depends on its midline α-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building block and on assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fiber assembly. SYCE2-TEX12’s building blocks are 2:2 coiled coils that dimerize into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibers that intertwine within 40-nm bundled micrometer-long fibers that define the SC’s midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behavior typical of cytoskeletal proteins to provide an α-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes.Crystallographic, electron microscopy and biophysical studies reveal how the synaptonemal complex component SYCE2-TEX12 undergoes self-assembly into fibrous supramolecular structures that mediate homologous chromosome synapsis in meiosis.
The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 [mu]m) depends on its midline [alpha]-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building block and on assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fiber assembly. SYCE2-TEX12's building blocks are 2:2 coiled coils that dimerize into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibers that intertwine within 40-nm bundled micrometer-long fibers that define the SC's midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behavior typical of cytoskeletal proteins to provide an [alpha]-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes.
The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 [mu]m) depends on its midline [alpha]-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building block and on assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fiber assembly. SYCE2-TEX12's building blocks are 2:2 coiled coils that dimerize into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibers that intertwine within 40-nm bundled micrometer-long fibers that define the SC's midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behavior typical of cytoskeletal proteins to provide an [alpha]-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes. Crystallographic, electron microscopy and biophysical studies reveal how the synaptonemal complex component SYCE2-TEX12 undergoes self-assembly into fibrous supramolecular structures that mediate homologous chromosome synapsis in meiosis.
The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 μm) depends on its midline α-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building block and on assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fiber assembly. SYCE2-TEX12's building blocks are 2:2 coiled coils that dimerize into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibers that intertwine within 40-nm bundled micrometer-long fibers that define the SC's midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behavior typical of cytoskeletal proteins to provide an α-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes.
The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 μm) depends on its midline α-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building-block and upon assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fibre assembly. SYCE2-TEX12’s building-blocks are 2:2 coiled-coils which dimerise into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibres, which intertwine within 40-nm bundled micrometre-long fibres that define the SC’s midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behaviour typical of cytoskeletal proteins to provide an α-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes.
The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along the chromosome length (up to 24 μm) depends on its midline α-fibrous component SYCE2-TEX12. Here, we report X-ray crystal structures of human SYCE2-TEX12 as an individual building block and on assembly within a fibrous lattice. We combine these structures with mutagenesis, biophysics and electron microscopy to reveal the hierarchical mechanism of SYCE2-TEX12 fiber assembly. SYCE2-TEX12’s building blocks are 2:2 coiled coils that dimerize into 4:4 hetero-oligomers and interact end-to-end and laterally to form 10-nm fibers that intertwine within 40-nm bundled micrometer-long fibers that define the SC’s midline structure. This assembly mechanism bears striking resemblance with intermediate filament proteins vimentin, lamin and keratin. Thus, SYCE2-TEX12 exhibits behavior typical of cytoskeletal proteins to provide an α-fibrous SC backbone that structurally underpins synaptic elongation along meiotic chromosomes. Crystallographic, electron microscopy and biophysical studies reveal how the synaptonemal complex component SYCE2-TEX12 undergoes self-assembly into fibrous supramolecular structures that mediate homologous chromosome synapsis in meiosis.
Audience Academic
Author Dunce, James M.
Salmon, Lucy J.
Davies, Owen R.
AuthorAffiliation 2 Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK
1 Wellcome Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK
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  givenname: Owen R.
  orcidid: 0000-0002-3806-5403
  surname: Davies
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  email: owen.davies@ed.ac.uk
  organization: Biosciences Institute, Faculty of Medical Sciences, Newcastle University, Framlington Place, Wellcome Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent
BackLink https://www.ncbi.nlm.nih.gov/pubmed/34373646$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
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PublicationTitleAbbrev Nat Struct Mol Biol
PublicationTitleAlternate Nat Struct Mol Biol
PublicationYear 2021
Publisher Nature Publishing Group US
Nature Publishing Group
Publisher_xml – name: Nature Publishing Group US
– name: Nature Publishing Group
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Snippet The synaptonemal complex (SC) is a supramolecular protein assembly that mediates synapsis between homologous chromosomes during meiosis. SC elongation along...
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631/535/1258
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82/29
82/80
82/83
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Biophysics
Cell Cycle Proteins - metabolism
Cell research
Cellular proteins
Chromosome Pairing - physiology
Chromosomes
Coils
Crystal structure
Crystallography
Crystallography, X-Ray
Cytoskeletal Proteins - metabolism
Cytoskeleton
Electron microscopy
Elongated structure
Elongation
Fibers
Homology
Humans
Keratin
Keratins - metabolism
Lamins - metabolism
Life Sciences
Long fibers
Meiosis
Meiosis - physiology
Membrane Biology
Microscopy
Mutagenesis
Oligomers
Protein Structure
Protein Structure, Quaternary
Proteins
Self-assembly
Structure
Synaptonemal complex
Synaptonemal Complex - metabolism
Vimentin
Vimentin - metabolism
Title Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12
URI https://link.springer.com/article/10.1038/s41594-021-00636-z
https://www.ncbi.nlm.nih.gov/pubmed/34373646
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https://pubmed.ncbi.nlm.nih.gov/PMC7612376
Volume 28
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