Mutation in dipZ leads to reduced production of active human placental alkaline phosphatase in Escherichia coli.
We have tested the expression of alkaline phosphatases in a mutant strain of Escherichia coli deficient in dipZ, a gene coding for a protein involved in cytochrome c biogenesis, and the isogenic wild-type strain. The yield of soluble and active human placental alkaline phosphatase was significantly reduced in the mutant but could be fully recovered by expression of dipZ subcloned in a vector with low copy number. Overexpression of E. coli alkaline phosphatase was unaffected in the mutant with or without dipZ co-expression.
Beck
R
R
Boehringer Mannheim Research Center, Penzberg, Germany.
Crooke
H
H
Jarsch
M
M
Cole
J
J
Burtscher
H
H
D000469:Alkaline Phosphatase / Q000096:biosynthesis* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics*; D005260:Female; D006801:Humans; D009154:Mutation; D010088:Oxidoreductases / Q000096:biosynthesis; D010920:Placenta / Q000201:enzymology; D010957:Plasmids; D011247:Pregnancy; D011994:Recombinant Proteins / Q000096:biosynthesis
D011994:Recombinant Proteins; D010088:Oxidoreductases; D000469:Alkaline Phosphatase