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Insertion of Single-pass Transmembrane Proteins in the RER01:26

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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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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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.
α-Helix containing multi-pass transmembrane proteins
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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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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Designed di-heme binding helical transmembrane protein.

Mukesh Mahajan1, Surajit Bhattacharjya

  • 1School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore-637551 (Singapore).

Chembiochem : a European Journal of Chemical Biology
|May 16, 2014
PubMed
Summary
This summary is machine-generated.

Researchers designed HETPRO, a novel transmembrane protein that binds heme and catalyzes redox reactions. This de novo designed protein offers insights into membrane protein stability and function.

Keywords:
NMR spectroscopyheme bindingmembrane proteinspeptidomimeticsperoxidases

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • De novo design of functional membrane proteins is crucial for understanding protein structure, folding, and stability.
  • Membrane proteins play vital roles in cellular processes, including electron transport and energy conversion.

Purpose of the Study:

  • To design and characterize a novel transmembrane protein, HETPRO (HEme-binding Transmembrane PROtein), capable of binding heme and catalyzing redox reactions.
  • To investigate the structural assembly and membrane integration of the designed protein.

Main Methods:

  • Guided optimization of a primary amino acid sequence derived from an antimicrobial peptide.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the structure of the apo form in detergent micelles.
  • Characterization of heme binding and catalytic activity.

Main Results:

  • HETPRO was successfully designed to orient within a membrane and exhibit defined structural properties.
  • HETPRO self-assembles into a tetrameric form from an apo dimeric helical structure upon cofactor binding.
  • NMR analysis revealed an antiparallel helical dimer structure for apo HETPRO, inserting into the micelle core.

Conclusions:

  • The designed HETPRO protein demonstrates a well-defined structure and the ability to bind heme, enabling catalytic redox functions.
  • HETPRO serves as a valuable model for functional membrane protein mimics, with potential applications in electron transport and artificial photosystems.