Elimination of truncated recombinant protein expressed in Escherichia coli by removing cryptic translation initiation site

Matthew J. Jennings, Adam F. Barrios, Song Tan

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Undesirable truncated recombinant protein products pose a special expression and purification challenge because such products often share similar chromatographic properties as the desired full length protein. We describe here our observation of both full length and a truncated form of a yeast protein (Gcn5) expressed in Escherichia coli, and the reduction or elimination of the truncated form by mutating a cryptic Shine-Dalgarno or START codon within the Gcn5 coding region. Unsuccessful attempts to engineer in a cryptic translation initiation site into other recombinant proteins suggest that cryptic Shine-Dalgarno or START codon sequences are necessary but not sufficient for cryptic translation in E. coli.

Original languageEnglish (US)
Pages (from-to)17-21
Number of pages5
JournalProtein Expression and Purification
Volume121
DOIs
StatePublished - May 1 2016

All Science Journal Classification (ASJC) codes

  • Biotechnology

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