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J Biol Chem, Vol. 273, Issue 41, 26349-26360, October 9, 1998

Structural Analysis of the fds Operon Encoding the NAD⁺-linked Formate Dehydrogenase of Ralstonia eutropha

From the Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Grisebachstrasse 8, D-37077 Göttingen, Germany

The fdsGBACD operon encoding the four subunits of the NAD⁺-reducing formate dehydrogenase of Ralstonia eutropha H16 was cloned and sequenced. Sequence comparisons indicated a high resemblance of FdsA (-subunit) to the catalytic subunits of formate dehydrogenases containing a molybdenum (or tungsten) cofactor. The NH₂-terminal region (residues 1-240) of FdsA, lacking in formate dehydrogenases not linked to NAD(P)⁺, exhibited considerable similarity to that of NuoG of the NADH:ubiquinone oxidoreductase from Escherichia coli as well as to HoxU and the NH₂-terminal segment of HndD of NAD(P)⁺-reducing hydrogenases. FdsB (-subunit) and FdsG (-subunit) are closely related to NuoF and NuoE, respectively, as well as to HoxF and HndA. It is proposed that the NH₂-terminal domain of FdsA together with FdsB and FdsG constitute a functional entity corresponding to the NADH dehydrogenase (diaphorase) part of NADH:ubiquinone oxidoreductase and the hydrogenases. No significant similarity to any known protein was observed for FdsD (-subunit). The predicted product of fdsC showed the highest resemblance to FdhD from E. coli, a protein required for the formation of active formate dehydrogenases in this organism. Transcription of the fds operon is subject to formate induction. A promoter structure resembling the consensus sequence of ⁷⁰-dependent promoters from E. coli was identified upstream of the transcriptional start site determined by primer extension analysis.

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