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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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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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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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Directionality of Nuclear Transport01:42

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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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Rab Proteins01:14

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Rapid Amplification of cDNA Ends, or RACE, is one of the most effective methods to obtain a full-length cDNA from an mRNA sequence between a known internal region to the unknown sequence at the 5’ or 3’ end. The unknown region is cloned in the cDNA by a gene-specific primer that binds the known end, and a hybrid primer that attaches a predefined anchor sequence to the unknown end of the cDNA. The sequence in between is amplified by PCR with an anchor primer and a gene-specific...
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Related Experiment Video

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A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA
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Structural basis for nuclear import complex dissociation by RanGTP.

Soo Jae Lee1, Yoshiyuki Matsuura, Sai Man Liu

  • 1MRC Laboratory of Molecular Biology, Hills Rd, Cambridge CB2 2QH, UK.

Nature
|May 3, 2005
PubMed
Summary
This summary is machine-generated.

Nuclear protein import relies on importin-beta and RanGTP. RanGTP binding to importin-beta alters its structure, releasing cargo and regulating nuclear transport.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • Nuclear protein import is essential for cellular function.
  • Importin-beta acts as a key transport factor, often utilizing importin-alpha as an adaptor.
  • RanGTP drives the disassembly of import complexes within the nucleus.

Purpose of the Study:

  • To elucidate the structural basis of nuclear import complex disassembly.
  • To understand the mechanism by which RanGTP releases cargo from importin-beta.

Main Methods:

  • X-ray crystallography was used to determine the structure of yeast importin-beta (Kap95p) complexed with RanGTP.
  • Analysis of the complex structure to identify key interaction interfaces.

Main Results:

  • The structure of full-length yeast importin-beta (Kap95p) complexed with RanGTP was determined.
  • A critical interaction site was identified between the RanGTP switch I loop and the carboxy-terminal arch of Kap95p.
  • This interaction induces a conformational change in Kap95p, preventing cargo binding.

Conclusions:

  • RanGTP binding to importin-beta causes an allosteric conformational change.
  • This mechanism explains how RanGTP facilitates cargo release during nuclear import.
  • The findings provide a structural basis for understanding nuclear transport regulation.