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Nucleic Acids Research, 1984, Vol. 12, No. 9 3937-3950
© 1984

MOLECULAR BIOLOGY

The influence of messenger RNA secondary structure on expression of an immunoglobulin heavy chain in Escherichia coli

Clive R. Wood, Michael A. Boss, Thakor P. Patel and J.Spencer Emtage

Celltech Ltd, 244–250 Bath Road, Slough SL1 4DY, Berks, UK

Received March 5, 1984. Accepted April 16, 1984.

A gene for murine a heavy chain immunoglobulin has been inserted into a bacterial expression plasmid containing the Eacherichia coli trp promoter and ribosome binding site. A low level expression of µ protein was detected. Secondary structure analysis showed the presence of a hairpin loop burying the µ initiation codon. Alteration of secondary structure at this site by oligonucleotide replacement mutagenesis revealed a correlation between µ expression levels and accessibility of the ribosome binding site. Abolition of secondary structure increased µ protein expression over ninety-fold, to a level approximately equal to that of a trpE-µ fusion protein using the native trpE ribosorae binding site.


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