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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Beyond Dimerization: Harnessing Tetrameric Coiled-Coils for Nanostructure Assembly.

Sara Vidmar1,2, Tamara Šmidlehner1, Jana Aupič1

  • 1Department of Synthetic Biology and Immunology, National Institute of Chemistry, Ljubljana, Slovenia.

Angewandte Chemie (International Ed. in English)
|December 12, 2024
PubMed
Summary
This summary is machine-generated.

Researchers designed novel protein nanostructures using tetrameric modules, enhancing stability and enabling the first 3D cryo-electron microscopy structure of such a coiled-coil nanostructure, a tetrahedral cage.

Keywords:
coiled-coilscryo-electron microscopyprotein designprotein origami

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Area of Science:

  • Biochemistry and structural biology
  • Nanotechnology and materials science

Background:

  • Modular nanostructures are typically built using DNA or polypeptide modules.
  • Previous designs often relied on coiled-coil dimerization units for structural assembly.
  • Polypeptides possess the capability to form higher-order oligomeric states beyond simple dimers.

Purpose of the Study:

  • To investigate the use of tetrameric modules as an alternative to coiled-coil dimerization in modular nanostructures.
  • To explore the potential of tetrameric modules to increase the complexity and stability of protein-based nanostructures.
  • To enable the construction of nanostructures from identical polypeptide chains.

Main Methods:

  • Design and synthesis of polypeptide modules incorporating tetramerizing helical bundles.
  • Assembly of nanostructures using these tetrameric modules in parallel or antiparallel orientations.
  • Cryo-electron microscopy (cryo-EM) for structural determination of the assembled nanostructures.
  • Assessment of nanostructure stability against air-water interface denaturation.

Main Results:

  • Tetrameric modules were successfully introduced as a substitute for coiled-coil dimerization units.
  • Tetramerizing helical bundles allowed for parallel and antiparallel orientations, increasing topological diversity.
  • The strategy facilitated the construction of nanostructures from two identical polypeptide chains.
  • Tetrameric modules significantly enhanced the stability of protein nanostructures against denaturation.
  • The first 3D cryo-electron microscopy structure of a coiled-coil-based nanostructure was determined, revealing a tetrahedral cage architecture.

Conclusions:

  • Tetrameric modules represent a versatile building block for advanced modular nanostructures.
  • This approach expands the design space for protein nanostructures, allowing for more complex architectures.
  • The enhanced stability provided by tetrameric modules is crucial for structural characterization techniques like cryo-EM.
  • The successful determination of the tetrahedral cage structure validates the design principles of tetramer-based modular assembly.