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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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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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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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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
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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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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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Dynamic Assembly of Pentamer-Based Protein Nanotubes.

Lukasz Koziej1, Farzad Fatehi2, Marta Aleksejczuk1

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Circularly permuted lumazine synthase (cpAaLS) forms hollow protein cages and nanotubes. Changes in ionic strength and subunit interactions drive the transformation, offering insights for designing novel nanoarchitectures.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Nanotechnology

Background:

  • Hollow protein particles serve as versatile nanocontainers for applications in delivery and catalysis.
  • Understanding the assembly principles of protein structures is crucial for designing functional nanomaterials.

Purpose of the Study:

  • To investigate the assembly mechanisms of a circularly permuted enzyme, Aquifex aeolicus lumazine synthase (cpAaLS).
  • To explore how ionic strength influences the morphology of cpAaLS assemblies.
  • To provide a theoretical and structural basis for designing protein-based nanoarchitectures.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) was used to determine the structures of assembled particles.
  • Circular permutation of Aquifex aeolicus lumazine synthase was employed.
  • Mathematical modeling was utilized to analyze subunit interactions and predict assembly patterns.

Main Results:

  • cpAaLS self-assembles into hollow spherical and cylindrical structures, adapting to varying ionic strengths.
  • These structures are exclusively composed of pentameric subunits.
  • The transformation from cages to tubes is driven by hindered 3-fold symmetry interactions and subunit torsion angles, mediated by an altered α-helix domain.
  • Mathematical models identified double- and triple-stranded helical arrangements as optimal tiling patterns.

Conclusions:

  • The study reveals dynamic assembly principles of pentamer-based protein cages and nanotubes.
  • Structural insights provide guidelines for engineering protein nanoarchitectures with tailored morphology and assembly properties.
  • Circular permutation offers a strategy to control protein assembly and create novel nanostructures.