Ubiquitin fusion technique and related methods

Methods Enzymol. 2005:399:777-99. doi: 10.1016/S0076-6879(05)99051-4.


The ubiquitin fusion technique, developed in 1986, is still the method of choice for producing a desired N-terminal residue in a protein of interest in vivo. This technique is also used as a tool for protein expression. Over the past two decades, several otherwise unrelated methods were invented that have in common the use of ubiquitin fusions as a component of design. I describe the original ubiquitin fusion technique, its current applications, and other methods that use the properties of ubiquitin fusions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Molecular Sequence Data
  • Protein Transport
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • Ubiquitin / chemistry
  • Ubiquitin / metabolism*


  • Recombinant Fusion Proteins
  • Ubiquitin