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Updated: Aug 21, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Relations and functions of dye-linked formaldehyde dehydrogenase from Hyphomicrobium zavarzinii revealed by sequence
Arnold C Schwartz1, Gaby Gockel, Julia Gross
1Institut für Molekulare Physiologie und Biotechnologie der Pflanzen, Universität Bonn, Kirschallee 1, 53115 Bonn, Germany. a.c.schwartz@uni-bonn.de
Abstract:
faoA, the gene of the dye-linked NAD(P)-independent quinone-containing formaldehyde dehydrogenase of methylamine-grown Hyphomicrobium zavarzinii strain ZV 580 was sequenced and analyzed together with an apparent promoter region and adjoining genes in a 7.2-kb fragment of hyphomicrobial DNA. The formaldehyde dehydrogenase, identified as a periplasmic enzyme by its signal sequence, is distantly related to the soluble pyrroloquinoline-quinone-dependent glucose dehydrogenase of Acinetobacter calcoaceticus and to other predicted glucose dehydrogenase sequences. The promoter region, containing about 400 nucleotides upstream of faoA, comprised potential binding sites identical or highly similar to known consensus sequences of the sigma factors sigma(70) (housekeeping), sigma(H) (heat shock), sigma(F) (flagellar) and sigma(N) (nitrogen). The complex regulation of the transcription of faoA, which is suggested by this setting and emphasized by a possible heat-shock promoter, supports a hypothesis proposing an auxiliary role of the enzyme in lowering detrimental elevated concentrations of formaldehyde, which might arise in the course of stress or regulatory transitions disturbing balanced C(1) metabolism.
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