PMID:22014167
| Citation |
Macomber, L, Elsey, SP and Hausinger, RP (2011) Fructose-1,6-bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli. Mol. Microbiol. 82:1291-300 |
|---|---|
| Abstract |
Nickel is toxic to all forms of life, but the mechanisms of cell damage are unknown. Indeed, environmentally relevant nickel levels (8 µM) inhibit wild-type Escherichia coli growth on glucose minimal medium. The same concentration of nickel also inhibits growth on fructose, but not succinate, lactate or glycerol; these results suggest that fructose-1,6-bisphosphate aldolase (FbaA) is a target of nickel toxicity. Cells stressed by 8 µM Ni(II) for 20 min lost 75% of their FbaA activity, demonstrating that FbaA is inactivated during nickel stress. Furthermore, overexpression of fbaA restored growth of an rcnA mutant in glucose minimal medium supplemented with 4 µM Ni(II), thus confirming that FbaA is a primary target of nickel toxicity. This class II aldolase has an active site zinc and a non-catalytic zinc nearby. Purified FbaA lost 80 % of its activity within 2 min when challenged with 8 µM Ni(II). Nickel-challenged FbaA lost 0.8 zinc and gained 0.8 nickel per inactivated monomer. FbaA mutants (D144A and E174A) affecting the non-catalytic zinc were resistant to nickel inhibition. These results define the primary site of nickel toxicity in E. coli as the class II aldolase FbaA through binding to the non-catalytic zinc site. |
| Links |
PubMed PMC3225726 Online version:10.1111/j.1365-2958.2011.07891.x |
| Keywords |
Carbohydrate Metabolism; Culture Media/chemistry; Enzyme Inhibitors/metabolism; Enzyme Inhibitors/toxicity; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/metabolism; Fructose-Bisphosphate Aldolase/antagonists & inhibitors; Fructose-Bisphosphate Aldolase/isolation & purification; Fructose-Bisphosphate Aldolase/metabolism; Kinetics; Mutant Proteins/antagonists & inhibitors; Mutant Proteins/metabolism; Nickel/metabolism; Nickel/toxicity |
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