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Literature summary for 2.7.7.65 extracted from

  • Lacanna, E.; Bigosch, C.; Kaever, V.; Boehm, A.; Becker, A.
    Evidence for Escherichia coli diguanylate cyclase DgcZ interlinking surface sensing and adhesion via multiple regulatory routes (2016), J. Bacteriol., 198, 2524-2535 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
paraquat enhances DgcZ-dependent biofilm formation in an FRD-dependent fashion Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
gene dgcZ, recombinant expression of an DgcZ-mVENUS fusion protein which localizes at one bacterial cell pole in response to alkaline pH and carbon starvation Escherichia coli

Protein Variants

Protein Variants Comment Organism
H79L/H83L site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme, cellular localization is unaltered Escherichia coli
H79L/H83L/E208Q site-directed mutagenesis, inactive mutant, cellular localization is unaltered Escherichia coli
additional information chromosomal replacement of the corresponding wild-type gene by mVENUS fusions to dgcZ wild-type or mutant variants, as well as by mCHERRY fusions to frdA and frdB, are achieved by standardFRED-mediated recombineering. In each case, the PRham-ccdB-kan element replaced the wild-type locus in the precursor strain. The dgcZ(+) and frdA(+) control strains are obtained by replacing the PRham-ccdBkan element with the dgcZ and frdA genes amplified from Escherichia coli strain MG1655 Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cell pole polar localization of DgcZ is independent of protein activity and concentration. Polar localization of DgcZ is induced by carbon starvation and alkaline pH Escherichia coli 60187
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additional information nutrient starvation or the accumulation of byproducts in the medium may result in polar localization of DgcZ in stationary phase. Restoring nutrient-sufficient conditions results in decreased levels and dispersed localization of DgcZ Escherichia coli
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-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ involved in enzyme activity regulation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 GTP Escherichia coli
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2 diphosphate + cyclic di-3',5'-guanylate
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli P31129
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 GTP
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Escherichia coli 2 diphosphate + cyclic di-3',5'-guanylate
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?

Synonyms

Synonyms Comment Organism
DgcZ
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Escherichia coli
YdeH
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Escherichia coli

Expression

Organism Comment Expression
Escherichia coli gene dgcZ transcription is activated by the transcriptional regulator CpxR up

General Information

General Information Comment Organism
malfunction nutrient starvation or the accumulation of byproducts in the medium may result in polar localization of DgcZ in stationary phase. Restoring nutrient-sufficient conditions results in decreased levels and dispersed localization of DgcZ Escherichia coli
metabolism DgcZ shows interaction with FrdB, a subunit of the fumarate reductase complex (FRD) involved in anaerobic respiration and in control of flagellum assembly, determined by coimmunoprecipitation analysis and bacterial-two-hybrid assay. The FRD complex is required for the increase in DgcZ-mediated biofilm formation upon induction of oxidative stress by addition of paraquat Escherichia coli
physiological function Escherichia coli diguanylate cyclase DgcZ interlinks surface sensing and adhesion via multiple regulatory routes. A FRD complex is required for the increase in DgcZ-mediated biofilm formation upon induction of oxidative stress by addition of paraquat. Possible integrative role of DgcZ in regulation of surface attachment. Both DgcZ-stimulated PGA biosynthesis and interaction of DgcZ with the FRD complex contribute to impeding bacterial escape from the surface. DgcZ is the main DGC involved in PGA production in Escherichia coli. Abundance and activity of DgcZ are regulated at several levels. Gene dgcZ transcription is activated by the transcriptional regulator CpxR. Beyond transcriptional and translational regulation of protein concentration, DgcZ activity is regulated by Zn2+. DgcZ localization and c-di-GMP concentrations change between transition and stationary phase Escherichia coli