Protein expression using ubiquitin fusion and cleavage.
Expressing proteins and polypeptides as fusions to ubiquitin offers the advantage of an often dramatic increase in yield, and the ability to produce any desired amino-terminal residue upon ubiquitin cleavage. The recent availability of cloned ubiquitin-cleaving enzymes has enhanced this technique for both bacterial and eukaryotic host systems.
Baker
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RT
Molecular Genetics Group, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT 2601, Australia. Rohan.Baker@anu.edu.au
D000818:Animals; D001483:Base Sequence; D001709:Biotechnology; D017931:DNA Primers / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005822:Genetic Vectors; D015394:Molecular Structure; D011401:Promoter Regions, Genetic; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics*; D014452:Ubiquitins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics*
D017931:DNA Primers; D011993:Recombinant Fusion Proteins; D014452:Ubiquitins