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Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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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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Nuclear Protein Sorting01:34

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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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Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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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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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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The Nucleosome Core Particle01:12

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Updated: Feb 26, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.

Natalia Bernardes1, Yuh Min Chook1

  • 1Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|February 25, 2026
PubMed
Summary
This summary is machine-generated.

Nuclear import receptors called importins are key for histone transport and folding. Recent studies reveal their dual roles in stabilizing histones and facilitating their delivery for nucleosome assembly.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Chromatin Biology

Background:

  • Nuclear import of histones and chromatin regulators is essential for DNA processes.
  • Histones require chaperones and import receptors for proper folding and chromatin deposition due to their basic and aggregation-prone nature.

Purpose of the Study:

  • To review recent advances in understanding the mechanisms of core and linker histone import and chaperoning.
  • To elucidate the roles of specific importins in histone nuclear transport and stabilization.

Main Methods:

  • Structural and biochemical studies were employed to investigate histone-importin interactions.
  • Analysis of Importin-4/Kap123, Importin-9/Kap114, and Importin-β-Importin-7 heterodimers.

Main Results:

  • Importin-4/Kap123 acts as both a transporter and chaperone for H3-H4 heterodimers, working with ASF1.
  • Importin-9/Kap114 imports H2A-H2B heterodimers via a RanGTP-insensitive mechanism, cooperating with Nap1.
  • Importin-β-Importin-7 mediates linker histone H1 import, highlighting importins' multifunctional roles.

Conclusions:

  • Importins are multifunctional, coupling histone stabilization, protection, nuclear import, and delivery for nucleosome assembly.
  • Further research is needed on secondary importins, histone modifications, and chaperone dynamics in histone trafficking and nucleosome assembly.