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Related Concept Videos

Nuclear Export01:42

Nuclear Export

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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.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
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Nuclear Export of mRNA02:31

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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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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.
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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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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Regulated mRNA Transport02:22

Regulated mRNA Transport

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In eukaryotes, transcription and translation are compartmentalized; an mRNA is first synthesized in the nucleus and then selectively transported to the cytoplasm for protein synthesis. Before transport, a pre-mRNA undergoes several steps of post-transcriptional modifications including splicing, 5' capping, and the addition of a poly-adenine tail. Various proteins bind to the pre-mRNA during these modifications. The mRNA transport takes place with the help of multiple proteins playing...
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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
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Ribosomes: lifting the nuclear export ban.

Arlen W Johnson1

  • 1Section of Molecular Genetics and Microbiology and the Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, USA.

Current Biology : CB
|February 8, 2014
PubMed
Summary
This summary is machine-generated.

Nuclear export of the large ribosomal subunit is controlled by a GTPase. This protein prevents the nuclear export factor Nmd3 from binding until the Rea1 AAA-ATPase remodels the pre-ribosome.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Ribosome Biogenesis

Background:

  • Nuclear export of the large ribosomal subunit is a critical step in ribosome biogenesis.
  • Efficient ribosome production is essential for cellular function and growth.

Purpose of the Study:

  • To investigate the regulatory mechanisms governing the nuclear export of the large ribosomal subunit.
  • To identify key proteins involved in pre-ribosome remodeling and export.

Main Methods:

  • Utilized biochemical assays to study protein interactions.
  • Employed genetic manipulation to analyze the roles of specific GTPases and ATPases.
  • Investigated ribosome assembly intermediates using microscopy and biochemical techniques.

Main Results:

  • Identified a GTPase that acts as a checkpoint for large ribosomal subunit export.
  • Demonstrated that this GTPase blocks the recruitment of the nuclear export factor Nmd3.
  • Showed that pre-ribosome remodeling by the AAA-ATPase Rea1 is required to release this block.

Conclusions:

  • Nuclear export of the large ribosomal subunit is tightly regulated by a GTPase-mediated checkpoint.
  • The AAA-ATPase Rea1 plays a crucial role in remodeling the pre-ribosome, enabling subsequent export.
  • This regulatory mechanism ensures the fidelity of ribosome biogenesis.