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Related Concept Videos

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,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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A B23-interacting sequence as a tool to visualize protein interactions in a cellular context.

Tanguy Lechertier1, Valentina Sirri, Danièle Hernandez-Verdun

  • 1Institut Jacques Monod, UMR 7592 CNRS/Universités Paris 6 et 7, 2 Place Jussieu, 75251 Paris Cedex 05, France.

Journal of Cell Science
|December 21, 2006
PubMed
Summary

Researchers identified a nucleolar localization sequence (NoLS) that targets proteins to the nucleolus. This NoLS binds to nucleolar protein B23, enabling visualization of protein interactions within cells.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The nucleolus is a key cellular organelle involved in ribosome biogenesis and other functions.
  • Understanding nucleolar protein localization and interactions is crucial for deciphering cellular processes.

Purpose of the Study:

  • To characterize a novel nucleolar localization sequence (NoLS).
  • To investigate the interaction of NoLS with nucleolar protein B23.
  • To explore the utility of NoLS as a tool for studying protein localization and interactions in vivo.

Main Methods:

  • In vitro binding assays to assess NoLS-B23 interaction.
  • In vivo studies using green fluorescent protein (GFP) fusions to track NoLS localization.
  • Drug treatments and protein fusions to perturb and observe cellular localization.

Main Results:

  • A specific NoLS was identified that directs GFP to the granular component of nucleoli.
  • NoLS directly and specifically binds to nucleolar protein B23 with high affinity.
  • In vivo experiments confirmed NoLS-B23 interaction and demonstrated NoLS-mediated relocalization of other proteins (fibrillarin, MafG) to nucleoli.

Conclusions:

  • The characterized NoLS serves as an effective tool for targeting proteins to the nucleolus.
  • NoLS-B23 interaction is a key determinant of nucleolar localization.
  • NoLS can be utilized to visualize and validate protein interactions within the cellular context.