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Related Concept Videos

Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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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.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
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Structure of Porins01:21

Structure of Porins

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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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Outer Layers of the Cell Envelope01:18

Outer Layers of the Cell Envelope

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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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The Resting Membrane Potential01:21

The Resting Membrane Potential

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Overview
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Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

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The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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Method for the Isolation of Francisella tularensis Outer Membranes
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Method for the Isolation of Francisella tularensis Outer Membranes

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Outer Membrane Porins.

Muriel Masi1, Mathias Winterhalter2, Jean-Marie Pagès3

  • 1UMR_MD1, Inserm U1261, IRBA, Membranes et Cibles Thérapeutiques, Facultés de Médecine et de Pharmacie, Aix-Marseille Université, Marseille, France.

Sub-Cellular Biochemistry
|June 20, 2019
PubMed
Summary
This summary is machine-generated.

Membrane transport proteins, like porins, are crucial for cell function. Recent studies reveal how these channels import small molecules, including antibiotics, across bacterial outer membranes, offering new therapeutic targets.

Keywords:
Antibiotic resistanceEnterobacteriaceaeEnvelope permeabilityOuter membrane protein biogenesisOuter membrane proteinsPorin regulationPorinsProtein channels

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From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
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Related Experiment Videos

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Method for the Isolation of Francisella tularensis Outer Membranes
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Size Exclusion Chromatography to Analyze Bacterial Outer Membrane Vesicle Heterogeneity
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From Constructs to Crystals &#8211; Towards Structure Determination of &#946;-barrel Outer Membrane Proteins
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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins

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Area of Science:

  • Molecular biology
  • Cellular biology
  • Biophysics

Background:

  • Membrane transport proteins facilitate essential cellular processes, including nutrient import and waste export.
  • Small polar molecules and ions require specialized proteins for membrane passage, unlike hydrophobic molecules.
  • Porins are a key class of non-specific diffusion channel proteins found in the outer membrane of Gram-negative bacteria.

Purpose of the Study:

  • To elucidate the mechanisms of small molecule uptake mediated by porins.
  • To review recent advancements in structural biology and functional assays related to porin function.
  • To explore the regulation of porin expression and biogenesis as potential therapeutic strategies.

Main Methods:

  • Structural biology techniques (e.g., X-ray crystallography, cryo-EM) to determine porin structures.
  • Functional assays to study the transport kinetics and specificity of porins.
  • Genetic and biochemical approaches to investigate porin regulation and biogenesis pathways.

Main Results:

  • Recent structural reports provide high-resolution insights into porin channel architecture and substrate translocation mechanisms.
  • Functional studies have clarified the role of porins in the uptake of various small molecules, including clinically relevant antibiotics.
  • Advances in understanding porin regulation and biogenesis have identified novel targets for antimicrobial drug development.

Conclusions:

  • Porins play a critical role in the selective permeability of the outer membrane, particularly for antibiotic entry into Enterobacteriaceae.
  • Detailed structural and functional understanding of porins is key to developing new therapeutic strategies.
  • Targeting porin expression and biogenesis pathways presents a promising avenue for combating bacterial infections.