Expression and rapid one-step purification of biologically active His-tagged factor C by Ni(2+) affinity column chromatography

Research output: Contribution to journalResearch articleContributedpeer-review


  • Z. Birkó - , University of Debrecen (Author)
  • F. Schauwecker - (Author)
  • F. Pfennig - , Technical University of Berlin (Author)
  • F. Szeszák - (Author)
  • S. Vitális - (Author)
  • Ullrich Keller - (Author)
  • S. Biró - (Author)


Factor C is an unusual extracellular protein capable of inducing cytodifferentiation in certain Streptomyces strains. The protein is produced by Streptomyces griseus 45H at such a low amount that the study of its mode of action was hindered by the shortage of purified protein. We report here the expression of C-terminally hexa-His-tagged factor C in Streptomyces lividans and Escherichia coli. Expression in S. lividans is low while in E. coli it is relatively high, yielding about 5--10 mg of biologically fully active protein per liter culture.


Original languageEnglish
Pages (from-to)223-227
Number of pages5
JournalFEMS microbiology letters
Issue number2
Publication statusPublished - 15 Mar 2001
Externally publishedYes

External IDs

Scopus 0035868619
ORCID /0000-0002-2331-2221/work/142242776



  • Amino Acid Sequence, Amino Acids/analysis, Bacterial Proteins/biosynthesis, Base Sequence, Chromatography, Affinity, Cloning, Molecular, DNA, Bacterial, Escherichia coli, Genes, Bacterial, Histidine/metabolism, Molecular Sequence Data, Recombinant Fusion Proteins/biosynthesis, Streptomyces griseus/genetics, Transformation, Bacterial

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