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Gene Review

fucO  -  L-1,2-propanediol oxidoreductase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2794, JW2770
 
 
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Disease relevance of fucO

 

High impact information on fucO

  • These mutants express the fucO gene constitutively, as a result of an IS5 insertion in the promoter region [1].
  • This phenotype is the result of the constitutive expression of the fucO gene (in the fucAO operon), which encodes one of the enzymes in the fucose metabolic pathway [2].
  • In general, when fucO becomes constitutively expressed, two other simultaneous changes occur: the fucA gene encoding fuculose-1-phosphate aldolase becomes constitutively expressed and the fucPIK operon encoding fucose permease, fucose isomerase, and fuculose kinase becomes noninducible [3].
  • Selection for increased aerobic growth rate on propanediol results in the escalation of basal synthesis of the NAD+-linked oxidoreductase encoded by fucO, a member of the fuc regulon for the utilization of L-fucose [3].
  • The induction of fucO transcription, which occurred in the presence of fucose, was confirmed by Northern blot analysis [4].
 

Chemical compound and disease context of fucO

 

Biological context of fucO

  • In the present study, we show that fucO and fucA form an operon which is divergently transcribed from the adjacent fucPIK operon [3].
 

Associations of fucO with chemical compounds

  • Anaerobically, lactaldehyde is reduced to L-1,2-propanediol by an NADH-linked oxidoreductase (fucO product) [7].
  • Mutations affecting this activity mapped to the ald locus at min 31, well apart from the fuc genes (min 60) encoding the trunk pathway for L-fucose dissimilation (as well as L-1,2-propanediol oxidoreductase) and the rha genes (min 88) encoding the trunk pathway for L-rhamnose dissimilation [8].
  • L-1,2-Propanediol oxidoreductase activity is inducible only anaerobically, and the effect of the two methylpentoses operates at different levels: L-fucose exerts its influence post-transcriptionally; L-rhamnose exerts its influence transcriptionally [9].

References

  1. Evolution of an Escherichia coli protein with increased resistance to oxidative stress. Lu, Z., Cabiscol, E., Obradors, N., Tamarit, J., Ros, J., Aguilar, J., Lin, E.C. J. Biol. Chem. (1998) [Pubmed]
  2. A cyclic AMP receptor protein mutant that constitutively activates an Escherichia coli promoter disrupted by an IS5 insertion. Podolny, V., Lin, E.C., Hochschild, A. J. Bacteriol. (1999) [Pubmed]
  3. Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol. Chen, Y.M., Lu, Z., Lin, E.C. J. Bacteriol. (1989) [Pubmed]
  4. Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae. Conway, T., Ingram, L.O. J. Bacteriol. (1989) [Pubmed]
  5. Constitutive activation of L-fucose genes by an unlinked mutation in Escherichia coli. Chen, Y.M., Chakrabarti, T., Lin, E.C. J. Bacteriol. (1984) [Pubmed]
  6. Use of operon fusions to examine the regulation of the L-1,2-propanediol oxidoreductase gene of the fucose system in Escherichia coli K12. Chen, Y.M., Lin, E.C., Ros, J., Aguilar, J. J. Gen. Microbiol. (1983) [Pubmed]
  7. L-1,2-propanediol exits more rapidly than L-lactaldehyde from Escherichia coli. Zhu, Y., Lin, E.C. J. Bacteriol. (1989) [Pubmed]
  8. NAD-linked aldehyde dehydrogenase for aerobic utilization of L-fucose and L-rhamnose by Escherichia coli. Chen, Y.M., Zhu, Y., Lin, E.C. J. Bacteriol. (1987) [Pubmed]
  9. Dual control of a common L-1,2-propanediol oxidoreductase by L-fucose and L-rhamnose in Escherichia coli. Chen, Y.M., Lin, E.C. J. Bacteriol. (1984) [Pubmed]
 
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