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Related Experiment Videos

Is this protein ubiquitinated?

Peter Kaiser1, Christian Tagwerker

  • 1Department of Biological Chemistry, University of California, Irvine, California, USA.

Methods in Enzymology
|December 13, 2005
PubMed
Summary
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Investigating protein ubiquitination is crucial for understanding cellular processes. This study details a method using hexahistidine-tagged ubiquitin to detect protein ubiquitination, even with low protein levels.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Protein ubiquitination is vital for numerous cellular functions.
  • Detecting protein ubiquitination in vivo is challenging due to low steady-state levels and active removal by proteasomes and deubiquitinating enzymes (Dubs).
  • Various methods exist to assess protein ubiquitination.

Purpose of the Study:

  • To present a reliable experimental approach for detecting protein ubiquitination.
  • To provide a method applicable to diverse research fields investigating ubiquitination.

Main Methods:

  • Utilizes the expression of hexahistidine-tagged ubiquitin.
  • Applies to situations where protein ubiquitination is suspected.
  • Successfully demonstrated in various organisms.

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Main Results:

  • The hexahistidine-tagged ubiquitin method facilitates the detection of ubiquitinated proteins.
  • This approach overcomes challenges associated with low ubiquitinated protein abundance.

Conclusions:

  • The hexahistidine-tagged ubiquitin method is a valuable tool for studying protein ubiquitination.
  • This technique can be widely applied across different biological systems to investigate ubiquitination.
  • It aids researchers in confirming ubiquitination of their proteins of interest.