Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination

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Abstract

In Escherichia coli biotin biosynthesis is repressed by high concentrations of exogenous biotin. This paper reports that upon high level production of the apo form of a biotinated protein, biotin operon expression was derepressed by 8-10-fold. The biotinated protein studied was the 1.3 S subunit of Propionibacterium shermanii, and transcarboxylase derepression was assayed by β-galactosidase production in strains which carry a lacZ gene altered such that it is transcribed from biotin operon promoters. Depression of β-galactosidase synthesis upon production of the apo 1.3 S protein was observed over a several hundred-fold range of biotin concentrations and also resulted in an increased level of biotin operon expression at maximally repressing biotin concentrations. Biotin operon derepression by apobiotin protein production seems a direct consequence of the properties of the biotin repressor protein which also functions as the ligase catalyzing the covalent attachment of biotin to apoproteins.

Original languageEnglish (US)
Pages (from-to)10332-10336
Number of pages5
JournalJournal of Biological Chemistry
Volume263
Issue number21
StatePublished - 1988

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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