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The F₄₂₀H₂-dehydrogenase from Methanolobus Tindarius: Cloning of the Ffd Operon and Expression of the Genes in Escherichia Coli
FEMS Microbiology Letters
  • David J. Westenberg, Missouri University of Science and Technology
  • Annett Braune
  • Claudia Ruppert
  • Volker Müller
  • Christina Herzberg
  • Gerhard Gottschalk
  • Michael Blaut
Abstract
The membrane-bound F420H2-dehydrogenase from the methylotrophic methanogen Methanolobus tindarius oxidizes reduced coenzyme F420 and feeds the electrons into an energy-conserving electron transport chain. Based on the N-terminal amino acid sequence of the 40-kDa subunit of F420H2-dehydrogenase the corresponding gene ffdB was detected in chromosomal DNA of M. Tindarius. Sequence analysis, primer extension, and RT-PCR experiments indicated that ffdB is part of an operon harboring three additional open reading frames (ffdA, ffdC, ffdD). The corresponding mRNA transcript and transcription start sites were determined. All four genes could be heterologously expressed in Escherichia coli.
Department(s)
Biological Sciences
Sponsor(s)
German Research Association
Fonds der Chemischen Industrie
Library of Congress Subject Headings
Electron transport
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 1999 John Wiley & Sons, All rights reserved.
Publication Date
1-1-1999
Disciplines
Citation Information
David J. Westenberg, Annett Braune, Claudia Ruppert, Volker Müller, et al.. "The F₄₂₀H₂-dehydrogenase from Methanolobus Tindarius: Cloning of the Ffd Operon and Expression of the Genes in Escherichia Coli" FEMS Microbiology Letters (1999)
Available at: http://works.bepress.com/david_westenberg/14/