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Applied and Environmental Microbiology, March 1999, p. 1092-1098, Vol. 65, No. 3
Department of Biochemistry and Microbiology,
Received 7 August 1998/Accepted 18 December 1998
Metal binding peptides of sequences Gly-His-His-Pro-His-Gly (named
HP) and Gly-Cys-Gly-Cys-Pro-Cys-Gly-Cys-Gly (named CP) were genetically
engineered into LamB protein and expressed in Escherichia
coli. The Cd2+-to-HP and Cd2+-to-CP
stoichiometries of peptides were 1:1 and 3:1, respectively. Hybrid LamB
proteins were found to be properly folded in the outer membrane of
E. coli. Isolated cell envelopes of E. coli
bearing newly added metal binding peptides showed an up to 1.8-fold
increase in Cd2+ binding capacity. The bioaccumulation of
Cd2+, Cu2+, and Zn2+ by E. coli was evaluated. Surface display of CP multiplied the ability
of E. coli to bind Cd2+ from growth medium
fourfold. Display of HP peptide did not contribute to an increase in
the accumulation of Cu2+ and Zn2+. However,
Cu2+ ceased contribution of HP for Cd2+
accumulation, probably due to the strong binding of Cu2+ to
HP. Thus, considering the cooperation of cell structures with inserted
peptides, the relative affinities of metal binding peptide and, for
example, the cell wall to metal ion should be taken into account in the
rational design of peptide sequences possessing specificity for a
particular metal.
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Enhanced Bioaccumulation of Heavy Metal Ions by Bacterial
Cells Due to Surface Display of Short Metal Binding
Peptides
ková,2
*
Corresponding author. Mailing address: Department of
Biochemistry and Microbiology, Institute of Chemical Technology,
Technická 3, 166 28 Prague, Czech Republic. Phone: (420)
2-24353022. Fax: (420) 2-3119990. E-mail:
TOMAS.RUML{at}VSCHT.CZ.
Applied and Environmental Microbiology, March 1999, p. 1092-1098, Vol. 65, No. 3
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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