The seleno-polypeptide of formic dehydrogenase (formate hydrogen-lyase linked) from Escherichia coli: genetic analysis.
The site of integration of phage M mu d (Ap lac) in mutant M9s which leads to deficiency of formic dehydrogenase (benzylviologen-linked) activity was determined. It was shown that the phage had inserted into the gene for the seleno-polypeptide of the enzyme (80 kd) leading to the formation of a truncated peptide (60 kd) still able to incorporate Se. Synthesis of the truncated polypeptide is subject to the same regulatory signals as that of the wild-type enzyme. The formation of the 110 kd seleno-polypeptide, which is a constituent component of the formic dehydrogenase from the formate-nitrate respiratory pathway, is unimpaired in mutant M9s. The location of the gene for the 80 kd seleno-polypeptide was mapped at 92.4 min of the Escherichia coli chromosome.
Pecher
A
A
Zinoni
F
F
Böck
A
A
D000445:Aldehyde Oxidoreductases / Q000235:genetics*; D001345:Autoradiography; D010583:Bacteriophage mu / Q000235:genetics; D002874:Chromosome Mapping; D002876:Chromosomes, Bacterial; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005560:Formate Dehydrogenases / Q000032:analysis / Q000235:genetics*; D005798:Genes, Bacterial; D005819:Genetic Markers; D010455:Peptides / Q000235:genetics; D012643:Selenium
D005819:Genetic Markers; D010455:Peptides; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; D012643:Selenium