Cyanobacterial metallothionein gene expressed in Escherichia coli Metal-binding properties of the expressed protein
The recently isolated Synechococcus gene smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the smtA gene was expressed in Escherichia coli as a car☐yterminal extension of glutathione- S-transferase....
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Veröffentlicht in: | FEBS letters 1992-06, Vol.303 (2), p.159-163 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The recently isolated Synechococcus gene
smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the
smtA gene was expressed in
Escherichia coli as a car☐yterminal extension of glutathione-
S-transferase. The pH of half dissociation of Zn, Cd and Cu ions from the expressed protein was determined to be 4.10, 3.50, 2.35, respectively, indicating a high affinity for these ions (in particular for Zn in comparison to mammalian MT).
E. coli expressing this gene showed enhanced (ca. 3-fold) accumulation of Zn. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(92)80509-F |