title: Protein expression using ubiquitin fusion and cleavage.
abstract: 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.
authors.affiliation: Molecular Genetics Group, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT 2601, Australia. Rohan.Baker@anu.edu.au
authors.forename: R T
authors.initials: RT
authors.lastname: Baker
mesh_terms: 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*
chemical_list: D017931:DNA Primers; D011993:Recombinant Fusion Proteins; D014452:Ubiquitins