A plant metallothionein produced in E. coli

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Abstract
A metallothionein cDNA was generated from pea (Pisum sativum L.) roots, amplified by PCR and inserted into a plasmid for expression in E. coli. Purification of the resultant product generated 3 pools of cadmium‐containing material after DEAE‐cellulose chromatography. The amino acid composition of each was in excellent agreement with that predicted for pea metallothionein. A cadmium content of ∼6 g.atoms per mole of protein was estimated. N‐terminal sequence analysis revealed that the recombinant molecule had been proteolysed within the extended region linking the 2 cysteine‐rich (putative) metal‐binding regions. The significance of these findings in terms of the protein folding/targeting of the molecule are considered.