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
Hauptverfasser: Shi, Jianguo, Lindsay, William P., Huckle, James W., Morby, Andrew P., Robinson, Nigel J.
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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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)80509-F