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Related Concept Videos

Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Substrate Sorting by a Supercharged Nanoreactor.

Yusuke Azuma1, Daniel L V Bader1, Donald Hilvert1

  • 1Laboratory of Organic Chemistry, ETH Zurich , 8093 Zurich, Switzerland.

Journal of the American Chemical Society
|December 27, 2017
PubMed
Summary
This summary is machine-generated.

Engineered protein cages with charged interiors can sort and degrade specific protein substrates. This nanoreactor technology enhances enzyme specificity for controlled protein degradation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nanotechnology

Background:

  • Cellular protein degradation relies on compartmentalization for spatiotemporal control.
  • Engineered protein cages offer potential for controlled enzymatic activity within confined spaces.

Purpose of the Study:

  • To investigate the use of a supercharged protein cage to control protease substrate specificity.
  • To demonstrate electrostatic sorting of substrates within a nanoreactor.

Main Methods:

  • Engineering a lumazine synthase protein cage with a negatively charged lumen.
  • Encapsulating a protease within the engineered cage.
  • Assessing substrate cleavage preference using polypeptides with varying charges.

Main Results:

  • The negatively supercharged nanochamber preferentially degraded positively charged polypeptides.
  • Substrate specificity of the encapsulated protease was inverted approximately 480-fold.
  • Electrostatic interactions within the cage dictated substrate selection.

Conclusions:

  • Supercharged nanochambers can confer substrate specificity to encapsulated enzymes.
  • This approach offers a general method for controlling catalyst activity through electrostatic sorting.
  • Potential applications in targeted protein degradation and synthetic biology.