Structural Analysis of thefdsOperon Encoding the NAD+-linked Formate Dehydrogenase ofRalstonia eutropha

Jeong-Il Oh, Botho Bowien
1998 Journal of Biological Chemistry  
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 NH 2 -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
more » ... idoreductase from Escherichia coli as well as to HoxU and the NH 2 -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 NH 2 -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.
doi:10.1074/jbc.273.41.26349 pmid:9756865 fatcat:wk6izmf3wbeyhcfqy5x2og6sbe