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Related Concept Videos

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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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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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The bacterial cell wall is an essential structural component that encases the plasma membrane, preserving cellular integrity, determining shape, and protecting against osmotic stress. This rigid yet flexible structure primarily comprises peptidoglycan, a polymer that forms a mesh-like matrix conferring mechanical strength and flexibility.Peptidoglycan Composition and StructurePeptidoglycan, the core of the bacterial cell wall, comprises alternating units of N-acetylglucosamine (NAG) and...
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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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Outer Layers of the Cell Envelope01:18

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The outermost layers of prokaryotic cells play a critical role in their survival, virulence, and interaction with the environment. These layers, often composed of polysaccharides, polypeptides, or proteins, form protective and adhesive structures that vary in organization and function.Capsules and Slime LayersCapsules are highly organized, tightly bound layers that firmly attach to the bacterial cell wall. Capsules are usually made of polysaccharides, though some are made of polypeptides. These...
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Fimbriae, Pili, and Axial Filaments01:28

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Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...
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Related Experiment Video

Updated: Oct 26, 2025

Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii
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Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii

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BonA from Acinetobacter baumannii Forms a Divisome-Localized Decamer That Supports Outer Envelope Function.

Rhys Grinter1, Faye C Morris1, Rhys A Dunstan1

  • 1Infection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash Universitygrid.1002.3, Clayton, Australia.

Mbio
|July 27, 2021
PubMed
Summary

Acinetobacter baumannii

Keywords:
Acinetobacter baumanniicell divisioncell envelopeouter membrane proteins

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Area of Science:

  • Microbiology
  • Structural Biology
  • Pathogen Research

Background:

  • Acinetobacter baumannii is a multidrug-resistant pathogen with a distinct cell envelope.
  • Understanding its unique resistance mechanisms is crucial for developing new treatments.

Purpose of the Study:

  • To investigate the structure and function of BonA, a novel outer membrane lipoprotein in A. baumannii.
  • To elucidate BonA's role in the bacterium's cell envelope and motility.

Main Methods:

  • X-ray crystallography, small-angle X-ray scattering, electron microscopy, and multiangle light scattering were used to determine BonA's structure.
  • Antisera were used to localize BonA within the bacterial cell.

Main Results:

  • BonA possesses a dual BON domain architecture and forms a transient decamer.
  • BonA is an outer membrane protein localized to the divisome and is essential for motility.
  • Loss of BonA affects outer membrane density and structure.

Conclusions:

  • BonA is a unique, dynamic protein essential for A. baumannii cell envelope integrity and motility.
  • Its structure and function provide insights into novel therapeutic targets for this critical pathogen.