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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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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.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Regulation of Nuclear Protein Sorting01:45

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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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Nuclear Export01:42

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Nuclear Localization Signals and Import01:46

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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Eukaryotic Compartmentalization01:37

Eukaryotic Compartmentalization

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One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles, such as the nucleus and mitochondria, that carry out specialized functions. Since biological membranes are only selectively permeable to solutes, they help create a compartment with controlled conditions inside an organelle. These microenvironments are tailored to the organelle's specific functions and help isolate them from the surrounding cytosol.
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Eukaryotic Compartmentalizations01:46

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One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles, such as the nucleus and mitochondria, that carry out specialized functions. Since biological membranes are only selectively permeable to solutes, they help create a compartment with controlled conditions inside an organelle. These microenvironments are tailored to the organelle's specific functions and help isolate them from the surrounding cytosol.
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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
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Comparative interactomics provides evidence for functional specialization of the nuclear pore complex.

Samson O Obado1, Mark C Field2, Michael P Rout1

  • 1a The Rockefeller University , New York , NY , USA.

Nucleus (Austin, Tex.)
|May 3, 2017
PubMed
Summary

The nuclear pore complex (NPC) scaffold is conserved across eukaryotes, but peripheral elements vary. Trypanosome NPCs lack mRNA export platforms, showing remarkable symmetry and suggesting stepwise NPC evolution.

Keywords:
Trypanosoma bruceieukaryogenesismRNA exportmolecular evolutionnuclear pore complex

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Area of Science:

  • Cell Biology
  • Evolutionary Biology
  • Structural Biology

Background:

  • The eukaryotic cell's core architecture, including the nuclear pore complex (NPC), is ancient but features lineage-specific adaptations.
  • The nuclear pore complex (NPC) regulates molecular transport and organizes the nucleus, with its structure well-characterized in Opisthokonts (e.g., yeast, humans).
  • Understanding NPC structural variation across diverse eukaryotic lineages remains limited.

Purpose of the Study:

  • To investigate the nuclear pore complex (NPC) architecture in trypanosomes, a highly divergent eukaryotic group.
  • To map trypanosome NPC proteins to substructures and compare their organization with other eukaryotes.
  • To elucidate the evolutionary history and functional implications of NPC structural diversity.

Main Methods:

  • Proteomic analysis of trypanosome nuclear pore complexes.
  • Bioinformatic mapping of NPC proteins to specific substructures.
  • Comparative structural analysis of NPCs across different eukaryotic taxa.

Main Results:

  • The central scaffold of the nuclear pore complex (NPC) is conserved in trypanosomes, suggesting universal conservation across eukaryotes.
  • Trypanosome NPCs exhibit significant lineage-specific alterations in peripheral components, including the absence of major mRNA export platform elements.
  • Trypanosome NPCs are predominantly symmetric, with the nuclear basket as the primary source of asymmetry.

Conclusions:

  • The nuclear pore complex (NPC) likely evolved stepwise, with an initial scaffold followed by the emergence of selective gating and peripheral remodeling machineries.
  • The observed NPC asymmetry in trypanosomes, particularly the lack of mRNA export platforms, highlights significant evolutionary divergence.
  • Comparative studies of NPC structure across eukaryotes are crucial for understanding fundamental biological processes and evolutionary trajectories.