Secretion of mouse-metallothionein by engineered E. coli cells in metal-enriched culture media.
Heterologous Escherichia coli expression systems were designed and assayed for the synthesis of functional mouse metallothionein (MT) as a secreted fusion protein. MT secretion was compared among different systems, and the optimum vector/host/medium combination was tested for metal removal. In this case, the Cu content of the medium decreased by up to 34% after growth of recombinant bacteria. The potential use of these genetically-engineered bacteria for water bioremediation is discussed as an alternative to cytoplasmic MT or membrane-bound MT heterologous expression systems.
Cols
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N
Departament de Genètica, Facultat de Biologia, Universitat de Barcelona, Spain.
Roepstorff
K
K
Gonzàlez-Duarte
R
R
Atrian
S
S
D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics; D001483:Base Sequence; D001673:Biodegradation, Environmental; D003300:Copper / Q000378:metabolism; D003470:Culture Media; D018076:DNA, Complementary / Q000235:genetics; D004785:Environmental Pollutants / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D005818:Genetic Engineering; D005822:Genetic Vectors; D008668:Metallothionein / Q000096:biosynthesis / Q000235:genetics*; D008670:Metals / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics
D001425:Bacterial Outer Membrane Proteins; D003470:Culture Media; D018076:DNA, Complementary; D004785:Environmental Pollutants; D008670:Metals; D011993:Recombinant Fusion Proteins; C078167:OMPA outer membrane proteins; D003300:Copper; D008668:Metallothionein