Ubiquitin fusion technique and related methods.
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.
Varshavsky
Alexander
A
Division of Biology, California, Institute of Technology, Pasadena, California, USA.
D000595:Amino Acid Sequence; D001483:Base Sequence; D008969:Molecular Sequence Data; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism*
D011993:Recombinant Fusion Proteins; D025801:Ubiquitin