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Related Concept Videos

Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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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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Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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How Tim proteins differentially exploit membrane features to attain robust target sensitivity.

Daniel Kerr1, Zhiliang Gong2, Tiffany Suwatthee3

  • 1Program in Biophysical Sciences, Institute for Biophysical Dynamics, Chicago, Illinois; Department of Chemistry, Chicago, Illinois; James Franck Institute, Chicago, Illinois.

Biophysical Journal
|September 16, 2021
PubMed
Summary
This summary is machine-generated.

Transmembrane immunoglobulin and mucin domain (Tim) proteins bind to cell membranes. This study quantifies how Tim1, Tim3, and Tim4 proteins selectively recognize anionic phospholipids like phosphatidylserine, revealing distinct binding behaviors.

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Area of Science:

  • Immunology
  • Biochemistry
  • Structural Biology

Background:

  • Immune cells use plasma membrane receptors to detect cellular changes.
  • Transmembrane immunoglobulin and mucin domain (Tim) proteins are key sensors of phosphatidylserine (PS) on activated cells.
  • The precise molecular mechanisms of Tim protein lipid recognition remain unclear.

Purpose of the Study:

  • To quantitatively compare the binding affinities and selectivities of murine Tim1, Tim3, and Tim4 proteins to anionic phospholipid membranes.
  • To elucidate the roles of electrostatic and hydrophobic interactions in Tim protein-membrane association.
  • To investigate the influence of other anionic lipids, such as phosphatidic acid, on Tim protein binding.

Main Methods:

  • Comparative quantitative analysis of protein-lipid interactions.
  • X-ray reflectivity and vesicle binding assays.
  • Development of a novel mathematical model for ligand interplay.

Main Results:

  • All three Tim proteins required calcium for membrane association.
  • Tim1, Tim3, and Tim4 exhibited distinct balances of hydrophobic and electrostatic interactions.
  • Phosphatidic acid significantly enhanced Tim3 and Tim4 binding, but not Tim1.
  • Protein binding showed varying sensitivity to phospholipid unsaturation and cooperativity with PS concentration.

Conclusions:

  • The three Tim protein homologs display contrasting selectivity in recognizing phospholipids on cell surfaces.
  • This differential recognition is governed by a complex interplay of electrostatic, hydrophobic, and cooperative ligand interactions.
  • The findings offer a generalizable model for peripheral protein-membrane binding dynamics.