CYANOBACTERIAL METALLOTHIONEIN GENE EXPRESSED IN ESCHERICHIA-COLI - METAL-BINDING PROPERTIES OF THE EXPRESSED PROTEIN

被引:51
作者
SHI, JG [1 ]
LINDSAY, WP [1 ]
HUCKLE, JW [1 ]
MORBY, AP [1 ]
ROBINSON, NJ [1 ]
机构
[1] UNIV DURHAM, DEPT BIOL SCI, DURHAM DH1 3LE, ENGLAND
关键词
SMTA; SMTA PROTEIN; PROKARYOTIC METALLOTHIONEIN; CYANOBACTERIA; SYNECHOCOCCUS; ANACYSTIS-NIDULANS; METAL-ACCUMULATION; METAL-TOLERANCE;
D O I
10.1016/0014-5793(92)80509-F
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Escherichica coli as a carboxyterminal 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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页码:159 / 163
页数:5
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