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Related Concept Videos

Septins01:19

Septins

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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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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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Role of Septins01:02

Role of Septins

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
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Binary Fission01:20

Binary Fission

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Fission is the division of a single entity into two or more parts, which regenerate into separate entities that resemble the original. Organisms in the Archaea and Bacteria domains reproduce using binary fission, in which a parent cell splits into two parts that can each grow to the size of the original parent cell. This asexual method of reproduction produces cells that are all genetically identical.
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The Contractile Ring02:15

The Contractile Ring

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Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
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The Phragmoplast01:59

The Phragmoplast

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Cell division is essential for organismal growth and development. In animal cells, the central spindle and its associated proteins form the midbody, a structure that has an essential role in cytokinesis. In plants, the central spindle, along with the microtubules, actin, and other cell components, matures into the phragmoplast, which is necessary for cytokinesis. Unlike the stationary midbody, the phragmoplast expands centrifugally, eventually leading to the formation of the new cell wall.
The...
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PcdA promotes orthogonal division plane selection in Staphylococcus aureus.

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Metabolic flux regulates growth transitions and antibiotic tolerance in uropathogenic <i>Escherichia coli</i>.

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Related Experiment Video

Updated: Jun 22, 2025

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

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Building the Bacterial Divisome at the Septum.

Josiah J Morrison1, Jodi L Camberg2

  • 1Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA.

Sub-Cellular Biochemistry
|July 4, 2024
PubMed
Summary

Bacterial cell division relies on FtsZ and FtsA proteins, homologs of eukaryotic tubulin and actin. These proteins assemble the divisome at the septum, ensuring accurate cell division and genetic material transfer.

Keywords:
ActinCell wallCytoskeletonDivision machineryDivisomePeptidoglycanSeptationTubulin

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Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Cell division is essential for life, conserving genetic material across generations.
  • Eukaryotic cell division utilizes tubulin (microtubules, mitotic spindle) and actin (cytoskeleton).
  • Prokaryotic cell division involves conserved homologs: FtsZ (tubulin homolog) and FtsA (actin homolog).

Purpose of the Study:

  • To discuss the functions of essential bacterial cell division proteins FtsZ and FtsA.
  • To elucidate their roles in assembling the divisome at the bacterial septum.
  • To explore regulatory mechanisms involving FtsZ and FtsA in bacterial division.

Main Methods:

  • Review of existing literature on FtsZ and FtsA functions.
  • Analysis of protein interactions and polymerization dynamics.
  • Discussion of regulatory protein roles in FtsZ and FtsA assembly.

Main Results:

  • FtsZ polymerizes at midcell, initiating divisome assembly and recruiting other proteins.
  • FtsA polymerizes and anchors FtsZ to the cytoplasmic membrane, facilitating septum formation.
  • FtsA interacts with later division proteins, crucial for cell wall synthesis.

Conclusions:

  • FtsZ and FtsA are essential, conserved proteins critical for bacterial cytokinesis.
  • Regulation of FtsZ polymerization and FtsA membrane association are key control points.
  • Ongoing research investigates FtsA's actin-like polymerization and its impact on division regulation.