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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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...
The Nucleolus02:55

The Nucleolus

The nucleolus is the most prominent substructure of the nucleus. When it was first discovered, it was considered to be an isolated organelle that forms fibrils and granules. In 1931, the relationship between the nucleolus and chromosomes was first described by Heitz. He observed that the appearance and size of nucleolus varies depending on the stage of the cell cycle. He also noticed constricted regions on different chromosomes clustered together at definite cell cycle stages. These regions,...
Nucleoid01:24

Nucleoid

The nucleoid represents a structurally and functionally distinct region within prokaryotic cells, where the cell's DNA and associated proteins are housed. Unlike eukaryotic cells, prokaryotes lack a membrane-bound nucleus, and the nucleoid facilitates the organization and accessibility of the genetic material within this constraint. The DNA in most bacteria and archaea exists as a single, circular, double-stranded molecule that is highly compacted through supercoiling and interactions with...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: Jun 4, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

PNAC: a protein nucleolar association classifier.

Michelle S Scott1, François-Michel Boisvert, Angus I Lamond

  • 1Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK. michelle@compbio.dundee.ac.uk

BMC Genomics
|January 29, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a new method to classify human proteins based on their dynamic association with the nucleolus, revealing its complex cellular roles. The findings provide a more accurate map of the nucleolar proteome.

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Area of Science:

  • Cell Biology
  • Proteomics
  • Bioinformatics

Background:

  • The nucleolus, primarily known for ribosome biogenesis, participates in diverse cellular functions.
  • Thousands of human proteins associate with the nucleolus, but their dynamic localization and the extent of association remain largely unknown.

Purpose of the Study:

  • To develop a computational method for classifying human proteins based on their dynamic nucleolar association.
  • To model the dynamic nature of the nucleolus and its proteome.

Main Methods:

  • A probabilistic predictor was trained using a curated literature-derived dataset of nucleolar-associated proteins.
  • The predictor integrates gene and protein characteristics to classify proteins into four groups: nucleolar-enriched, nucleolar-nucleoplasmic, nucleolar-cytoplasmic, or non-nucleolar.

Main Results:

  • The predictor achieved high accuracy (0.85 on a test set) in classifying protein localization.
  • The classification identified distinct Gene Ontology biological process signatures and evolutionary characteristics for different nucleolar association groups.
  • The study provides a dynamic model of nucleolar content, moving beyond static lists of proteins.

Conclusions:

  • The proteome-wide classification offers a novel and dynamic representation of the nucleolus.
  • This approach enhances the accuracy and specificity of nucleolar proteome annotation.
  • The findings will aid in understanding the nucleolus's central role and its interactions with other cellular compartments.