The F₄₂₀H₂-dehydrogenase from Methanolobus Tindarius: Cloning of the Ffd Operon and Expression of the Genes in Escherichia Coli
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.
Recommended Citation
D. J. Westenberg et al., "The F₄₂₀H₂-dehydrogenase from Methanolobus Tindarius: Cloning of the Ffd Operon and Expression of the Genes in Escherichia Coli," FEMS Microbiology Letters, vol. 170, no. 2, pp. 389 - 398, John Wiley & Sons, Jan 1999.
The definitive version is available at https://doi.org/10.1111/j.1574-6968.1999.tb13399.x
Department(s)
Biological Sciences
Sponsor(s)
German Research Association
Fonds der Chemischen Industrie
Keywords and Phrases
Electron Transport; F420H2-dehydrogenase; ffdB Gene; Heterologous Expression; Methanolobus tindarius
International Standard Serial Number (ISSN)
0378-1097;1574-6968
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 1999 John Wiley & Sons, All rights reserved.
Publication Date
01 Jan 1999
PubMed ID
9933933
Comments
The financial support by the "Deutsche Forschungsgemeinschaft" and "Fonds der ChemischenIndustrie" is gratefully acknowledged.