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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Generation of Straight or Branched Actin Filaments01:14

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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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As cells progress into mitosis, the nuclear envelope breaks down, and the condensed chromosomes are exposed to the array of bipolar microtubules of the mitotic spindle. The kinetochore, a large, disc-shaped protein complex, is present at the centromere region of the sister chromatids and acts as a binding site for the microtubules.  Usually, the plus-end of a single microtubule is embedded within the kinetochore. However, some kinetochores first establish lateral contact with the side-wall...
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During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
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Archaeal surface appendages are highly specialized structures essential for environmental adaptation, encompassing roles in adhesion, biofilm formation, and motility. Among these appendages, pili and archaella stand out for their distinct morphologies and functionalities, enabling archaea to thrive in diverse and often extreme environments.Pili: Adhesion and Biofilm FormationPili are filamentous structures assembled from pilin protein subunits, primarily contributing to adhesion and biofilm...
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How and Why Chaperone-Usher Pilus Rods Stretch.

Hye-Jeong Yeo1

  • 1Department of Biology and Biochemistry, University of Houston, Houston, TX 77204, USA.

Structure (London, England : 1993)
|December 7, 2017
PubMed
Summary

Uropathogenic Escherichia coli use type 1 and P pili to cause urinary tract infections. Researchers visualized the type 1 pilus rod structure, revealing molecular details of pilus uncoiling.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biophysics

Background:

  • Uropathogenic Escherichia coli (UPEC) are the primary cause of urinary tract infections (UTIs).
  • Type 1 and P pili are critical virulence factors enabling UPEC adherence and infection progression.
  • Understanding the structure and mechanics of these pili is crucial for developing targeted therapies.

Purpose of the Study:

  • To determine the near-atomic resolution structure of the type 1 pilus rod.
  • To elucidate the molecular mechanisms underlying pilus rod uncoiling.
  • To provide insights into the mechanical properties of type 1 pili.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to obtain high-resolution structural data.
  • Image processing and computational modeling were used to reconstruct the pilus rod structure.

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  • Structural analysis focused on identifying conformational changes related to uncoiling.

    • Main Results:

    • A near-atomic resolution structure of the type 1 pilus rod was successfully determined.
    • The structure revealed distinct conformations suggesting a mechanism for rod uncoiling.
    • Specific molecular interactions involved in pilus flexibility were identified.

    Conclusions:

    • The study provides unprecedented molecular detail of the type 1 pilus rod structure.
    • Insights into pilus uncoiling offer a basis for understanding UPEC virulence.
    • This structural information may inform the design of novel anti-adhesion strategies against UTIs.