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Related Concept Videos

Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

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Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
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Introduction to Actin01:26

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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
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Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order 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.
The high-order actin...
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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Bacterial Actins and Their Interactors.

Pananghat Gayathri1

  • 1Indian Institute of Science Education and Research (IISER Pune), Dr. Homi Bhabha Road, Pune, 411008, India. gayathri@iiserpune.ac.in.

Current Topics in Microbiology and Immunology
|November 7, 2016
PubMed
Summary

Bacterial actins are crucial for cell functions, exhibiting diverse dynamics influenced by interacting partners. Understanding these interactions reveals how bacterial actin filaments perform essential cellular roles.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Bacterial actins polymerize like eukaryotic actin, utilizing nucleotide binding (ATP) and hydrolysis.
  • They exhibit diverse protofilament arrangements and dynamics, unlike eukaryotic actin.
  • These filaments are vital for bacterial cell shape, division, plasmid segregation, and organelle positioning.

Purpose of the Study:

  • To review structural and functional aspects of bacterial actins.
  • To focus on the impact of interacting partners on bacterial actin filament dynamics.
  • To elucidate how these interactions facilitate bacterial cellular functions.

Main Methods:

  • Review of existing literature on bacterial actin structures and dynamics.
  • Analysis of polymerization mechanisms and nucleotide hydrolysis.

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  • Examination of known interacting partners and their effects.

    • Main Results:

    • Bacterial actins display varied protofilament arrangements and polymerization dynamics.
    • Filament stability is influenced by nucleotide-bound state (ATP vs. ADP) and monomer addition rates.
    • Interacting partners significantly modulate bacterial actin filament dynamics, though this is less studied.

    Conclusions:

    • Bacterial actin filament dynamics are complex and influenced by nucleotide state and interacting proteins.
    • Understanding these dynamics and interactions is key to comprehending bacterial cell biology.
    • Further research into interacting partners will illuminate diverse bacterial actin functions.