D-galactose catabolism in archaea: operation of the DeLey–Doudoroff pathway in Haloferax volcanii. Issue 1 (14th February 2020)
- Record Type:
- Journal Article
- Title:
- D-galactose catabolism in archaea: operation of the DeLey–Doudoroff pathway in Haloferax volcanii. Issue 1 (14th February 2020)
- Main Title:
- D-galactose catabolism in archaea: operation of the DeLey–Doudoroff pathway in Haloferax volcanii
- Authors:
- Tästensen, Julia-Beate
Johnsen, Ulrike
Reinhardt, Andreas
Ortjohann, Marius
Schönheit, Peter - Abstract:
- ABSTRACT: The haloarchaeon Haloferax volcanii was found to grow on D-galactose as carbon and energy source. Here we report a comprehensive analysis of D-galactose catabolism in H. volcanii . Genome analyses indicated a cluster of genes encoding putative enzymes of the DeLey–Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase. The recombinant galactose dehydrogenase and galactonate dehydratase showed high specificity for D-galactose and galactonate, respectively, whereas KDPGal aldolase was promiscuous in utilizing KDPGal and also the C4 epimer 2-keto-3-deoxy-6-phosphogluconate as substrates. Growth studies with knock-out mutants indicated the functional involvement of galactose dehydrogenase, galactonate dehydratase and KDPGal aldolase in D-galactose degradation. Further, the transcriptional regulator GacR was identified, which was characterized as an activator of genes of the DeLey–Doudoroff pathway. Finally, genes were identified encoding components of an ABC transporter and a knock-out mutant of the substrate binding protein indicated the functional involvement of this transporter in D-galactose uptake. This is the first report of D-galactose degradation via the DeLey–Doudoroff pathway in the domain of archaea. Abstract : Galactose uptake and degradation in Haloferax volcanii proceed via an ABC transporter and enzymes of theABSTRACT: The haloarchaeon Haloferax volcanii was found to grow on D-galactose as carbon and energy source. Here we report a comprehensive analysis of D-galactose catabolism in H. volcanii . Genome analyses indicated a cluster of genes encoding putative enzymes of the DeLey–Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase. The recombinant galactose dehydrogenase and galactonate dehydratase showed high specificity for D-galactose and galactonate, respectively, whereas KDPGal aldolase was promiscuous in utilizing KDPGal and also the C4 epimer 2-keto-3-deoxy-6-phosphogluconate as substrates. Growth studies with knock-out mutants indicated the functional involvement of galactose dehydrogenase, galactonate dehydratase and KDPGal aldolase in D-galactose degradation. Further, the transcriptional regulator GacR was identified, which was characterized as an activator of genes of the DeLey–Doudoroff pathway. Finally, genes were identified encoding components of an ABC transporter and a knock-out mutant of the substrate binding protein indicated the functional involvement of this transporter in D-galactose uptake. This is the first report of D-galactose degradation via the DeLey–Doudoroff pathway in the domain of archaea. Abstract : Galactose uptake and degradation in Haloferax volcanii proceed via an ABC transporter and enzymes of the DeLey–Doudoroff pathway. … (more)
- Is Part Of:
- FEMS microbiology letters. Volume 367:Issue 1(2020)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 367:Issue 1(2020)
- Issue Display:
- Volume 367, Issue 1 (2020)
- Year:
- 2020
- Volume:
- 367
- Issue:
- 1
- Issue Sort Value:
- 2020-0367-0001-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-02-14
- Subjects:
- Haloferax volcanii -- D-galactose -- archaea -- DeLey–Doudoroff pathway -- ABC transporter -- IclR like transcriptional regulator
Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1093/femsle/fnaa029 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25827.xml