A plant metallothionein produced in E. coli.

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 approximately 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kille P,Winge DR,Harwood JL,Kay J

doi

10.1016/0014-5793(91)81411-z

subject

Has Abstract

pub_date

1991-12-16 00:00:00

pages

171-5

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)81411-Z

journal_volume

295

pub_type

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