Plasmids pTugA and pTugAS, designed for expression of cloned genes in
Escherichia coli, possess the features of high-level inducible transcr
iption, enhanced RNA translation, portability, high copy number, stabi
lity and versatility. In addition, pTugAS can be used to produce fusio
n proteins comprising a target protein and a cellulose-binding domain.
Such fusion proteins can be purified in a single step by affinity chr
omatography on cellulose. Expression of two model gene fusions using t
he pTug plasmids resulted in yields of 500 mg of intracellular and 250
mg of extracellular recombinant protein per liter.