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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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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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The protrusion of the cell surface is an initial step for several cellular processes, including cell migration, phagocytosis, and neurite outgrowth. These membrane protrusions are a result of cytoskeletal rearrangement. The most  widely observed cell protrusions include lamellipodia, pseudopodia, filopodia, microvilli, invadopodia, and podosomes. These protrusions can be of two types — static or dynamic.
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Updated: May 29, 2025

Nanopodia - Thin, Fragile Membrane Projections with Roles in Cell Movement and Intercellular Interactions
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Multimodal Membrane Poration by Thanatin.

Alex Hoose1, Javier Garcia-Ruiz1,2, Corrin Blake3,4

  • 1National Physical Laboratory, Hampton Road, Teddington TW11 0LW, U.K.

Langmuir : the ACS Journal of Surfaces and Colloids
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This summary is machine-generated.

Thanatin, a novel antimicrobial peptide, creates membrane pores and channels, offering a multimodal mechanism against resistant bacteria. This finding provides insight into new antimicrobial strategies.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Antimicrobial resistance necessitates novel agents with multimodal mechanisms.
  • Host defense peptides and bacteriocins are promising candidates.
  • Thanatin exhibits properties of both classes, including stability and broad-spectrum activity.

Purpose of the Study:

  • To investigate the membrane interaction mechanism of thanatin.
  • To determine if thanatin induces bacteriocin-like poration in phospholipid bilayers.
  • To provide direct observation of thanatin's effect on membranes.

Main Methods:

  • Studied thanatin's interaction with phospholipid bilayers.
  • Analyzed membrane thinning, fractal ruptures, and channel formation.
  • Compared thanatin's mechanism to known antimicrobial peptides and bacteriocins.

Main Results:

  • Thanatin induces multimodal poration in phospholipid bilayers.
  • Observed membrane thinning and fractal ruptures upon thanatin interaction.
  • Demonstrated the formation of transmembrane channels by thanatin.
  • Thanatin's membrane effects are characteristic of bacteriocins, not typical antimicrobial peptides.

Conclusions:

  • Thanatin acts via bacteriocin-like multimodal poration, distinct from typical antimicrobial peptides.
  • Mechanistic insights into thanatin's action contribute to understanding diverse antimicrobial agent properties.
  • This study provides a direct observation of thanatin's membrane-disrupting capabilities.