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 trun...

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Bibliographic Details
Published inArchives of microbiology Vol. 141; no. 4; p. 359
Main Authors Pecher, A, Zinoni, F, Böck, A
Format Journal Article
LanguageEnglish
Published Germany 01.05.1985
Subjects
Aldehyde Oxidoreductases - genetics
Autoradiography
Bacteriophage mu - genetics
Chromosome Mapping
Chromosomes, Bacterial
Escherichia coli - enzymology
Escherichia coli - genetics
Formate Dehydrogenases - analysis
Formate Dehydrogenases - genetics
Genes, Bacterial
Genetic Markers
Peptides - genetics
Selenium
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Summary: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.
ISSN:0302-8933
DOI:10.1007/BF00428850