In-frame fusion of a His-Cys motif into the Pseudomonas aeruginosa outer membrane OprI lipoprotein results in increased metal binding capacity by Escherichia coli.
OprI, a small outer membrane lipoprotein from Pseudomonas aeruginosa, can be produced in large amounts and anchored at the surface on Escherichia coli cells. A four-time repeated (His-Cys) motif was fused to the C-terminal part of OprI. After induction, E. coli cells harbouring the recombinant oprI gene became more sensitive to Cd and Co. The same cells, after IPTG induction, bound four to eight times more Cd and Cr than control cells expressing oprI alone.
Bouia
A
A
Department de Biologie, Faculté des Sciences Dhar Mehrez, Fès, Morocco.
Kholti
A
A
Saghi
M
M
Cornelis
P
P
D020816:Amino Acid Motifs / Q000235:genetics / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003470:Culture Media; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008074:Lipoproteins / Q000235:genetics / Q000378:metabolism*; D019216:Metals, Heavy / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D003470:Culture Media; D008074:Lipoproteins; D019216:Metals, Heavy; D011993:Recombinant Fusion Proteins; C060507:outer membrane lipoprotein I, Bacteria