Functional expression of the yeast Mn-superoxide dismutase gene in Escherichia coli requires deletion of the signal peptide sequence.
Oligodeoxyribonucleotide-directed mutagenesis has been used to delete the leader sequence-coding region from the yeast gene specifying Mn-superoxide dismutase and thus enable its expression in Escherichia coli. The deletion of this leader was demonstrated to be an absolute requirement for the synthesis of an active yeast enzyme in the bacterium. Complementation analysis in E. coli has confirmed that the product of the truncated yeast gene is active in vivo as well as in vitro.
Schrank
I S
IS
Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, U.K.
Sims
P F
PF
Oliver
S G
SG
D000595:Amino Acid Sequence; D001483:Base Sequence; D002872:Chromosome Deletion; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005800:Genes, Fungal; D007700:Kinetics; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D010957:Plasmids; D021382:Protein Sorting Signals / Q000235:genetics*; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D013482:Superoxide Dismutase / Q000235:genetics* / Q000378:metabolism
D015345:Oligonucleotide Probes; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D013482:Superoxide Dismutase