Polylinker-encoded peptides can confer toxicity to recombinant proteins produced in Escherichia coli

E. Viaplana, A. Villaverde

Research output: Contribution to journalArticleResearchpeer-review

16 Citations (Scopus)

Abstract

Three DNA segments encoding fragments of the p60 capsid protein of rabbit haemorrhagic disease virus (RHDV) have been cloned and expressed in Escherichia coli. The cDNAs were placed under the control of the T7 promoter in a pET-derived expression vector designed to produce C-terminal histidine tail fusions. By using different cloning strategies, cell toxicity exhibited by some of the expressed products was dramatically affected, coincident with minor modifications in the carboxy terminus sequences of the recombinant proteins. In particular, the presence of a nonhydrophobic peptide encoded by polylinker sequences promotes cell death and a reduced yield after induction of gene expression, whereas a histidine tail has no detectable effect. These data point out the critical role that needless peptide tails, accidentally introduced into recombinant proteins by nonrelevant DNA stretches, can have on protein expression and final yield of a production process.
Original languageEnglish
Pages (from-to)723-727
JournalBiotechnol. Prog.
Volume0
Issue number12
DOIs
Publication statusPublished - 1 Sep 1996

Fingerprint Dive into the research topics of 'Polylinker-encoded peptides can confer toxicity to recombinant proteins produced in Escherichia coli'. Together they form a unique fingerprint.

Cite this