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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-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...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Related Experiment Video

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Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

Detecting protein-protein interactions with the Split-Ubiquitin sensor.

Alexander Dünkler1, Judith Müller, Nils Johnsson

  • 1Department of Biology, Institute of Molecular Genetics and Cell Biology, Ulm University, Ulm, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|September 23, 2011
PubMed
Summary

The Split-Ubiquitin technique detects protein interactions by reconstituting ubiquitin fragments. This method screens yeast for interaction partners of various proteins, including transcription factors and membrane proteins.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Yeast Genetics

Background:

  • Understanding cellular processes necessitates knowledge of protein-protein interactions.
  • Identifying protein interactions is crucial for deciphering complex biological pathways.

Purpose of the Study:

  • To present methods for monitoring and detecting protein interactions using the Split-Ubiquitin technique.
  • To enable screening for interaction partners of diverse proteins in yeast.

Main Methods:

  • Utilizing the Split-Ubiquitin technique, which relies on reconstituting ubiquitin from N- and C-terminal fragments.
  • Employing Ura3p as a reporter for ubiquitin fragment reconstitution.
  • Screening yeast using either a randomly generated expression library or a defined array of protein fusions.

Main Results:

  • Demonstrated the capability of the Split-Ubiquitin technique to detect interactions involving transcription factors and membrane-associated proteins.
  • Successfully developed methods for screening interaction partners in yeast.

Conclusions:

  • The Split-Ubiquitin technique is a versatile tool for identifying protein-protein interactions.
  • This method facilitates the discovery of interaction partners for a wide range of proteins in a yeast model system.