A cAMP/CRP-controlled mechanism for the incorporation of extracellular ADP-glucose in Escherichia coli involving NupC and NupG nucleoside transporters. Issue 1 (December 2018)
- Record Type:
- Journal Article
- Title:
- A cAMP/CRP-controlled mechanism for the incorporation of extracellular ADP-glucose in Escherichia coli involving NupC and NupG nucleoside transporters. Issue 1 (December 2018)
- Main Title:
- A cAMP/CRP-controlled mechanism for the incorporation of extracellular ADP-glucose in Escherichia coli involving NupC and NupG nucleoside transporters
- Authors:
- Almagro, Goizeder
Viale, Alejandro
Montero, Manuel
Muñoz, Francisco
Baroja-Fernández, Edurne
Mori, Hirotada
Pozueta-Romero, Javier - Abstract:
- Abstract ADP-glucose is the precursor of glycogen biosynthesis in bacteria, and a compound abundant in the starchy plant organs ingested by many mammals. Here we show that the enteric speciesEscherichia coli is capable of scavenging exogenous ADP-glucose for use as a glycosyl donor in glycogen biosynthesis and feed the adenine nucleotide pool. To unravel the molecular mechanisms involved in this process, we screened theE .coli single-gene deletion mutants of the Keio collection for glycogen content in ADP-glucose-containing culture medium. In comparison to wild-type (WT) cells, individual∆nupC and∆nupG mutants lacking the cAMP/CRP responsive inner-membrane nucleoside transporters NupC and NupG displayed reduced glycogen contents and slow ADP-glucose incorporation. In concordance, ∆cya and∆crp mutants accumulated low levels of glycogen and slowly incorporated ADP-glucose. Two-thirds of the glycogen-excess mutants identified during screening lacked functions that underlie envelope biogenesis and integrity, including the RpoE specific RseA anti-sigma factor. These mutants exhibited higher ADP-glucose uptake than WT cells. The incorporation of either∆crp, ∆nupG or∆nupC null alleles sharply reduced the ADP-glucose incorporation and glycogen content initially witnessed in∆rseA cells. Overall, the data showed thatE .coli incorporates extracellular ADP-glucose through a cAMP/CRP-regulated process involving the NupC and NupG nucleoside transporters that is facilitated under envelopeAbstract ADP-glucose is the precursor of glycogen biosynthesis in bacteria, and a compound abundant in the starchy plant organs ingested by many mammals. Here we show that the enteric speciesEscherichia coli is capable of scavenging exogenous ADP-glucose for use as a glycosyl donor in glycogen biosynthesis and feed the adenine nucleotide pool. To unravel the molecular mechanisms involved in this process, we screened theE .coli single-gene deletion mutants of the Keio collection for glycogen content in ADP-glucose-containing culture medium. In comparison to wild-type (WT) cells, individual∆nupC and∆nupG mutants lacking the cAMP/CRP responsive inner-membrane nucleoside transporters NupC and NupG displayed reduced glycogen contents and slow ADP-glucose incorporation. In concordance, ∆cya and∆crp mutants accumulated low levels of glycogen and slowly incorporated ADP-glucose. Two-thirds of the glycogen-excess mutants identified during screening lacked functions that underlie envelope biogenesis and integrity, including the RpoE specific RseA anti-sigma factor. These mutants exhibited higher ADP-glucose uptake than WT cells. The incorporation of either∆crp, ∆nupG or∆nupC null alleles sharply reduced the ADP-glucose incorporation and glycogen content initially witnessed in∆rseA cells. Overall, the data showed thatE .coli incorporates extracellular ADP-glucose through a cAMP/CRP-regulated process involving the NupC and NupG nucleoside transporters that is facilitated under envelope stress conditions. … (more)
- Is Part Of:
- Scientific reports. Volume 8:Issue 1(2018)
- Journal:
- Scientific reports
- Issue:
- Volume 8:Issue 1(2018)
- Issue Display:
- Volume 8, Issue 1 (2018)
- Year:
- 2018
- Volume:
- 8
- Issue:
- 1
- Issue Sort Value:
- 2018-0008-0001-0000
- Page Start:
- 1
- Page End:
- 15
- Publication Date:
- 2018-12
- Subjects:
- Natural history -- Research -- Periodicals
Biology -- Research -- Periodicals
Physical sciences -- Research -- Periodicals
Earth sciences -- Research -- Periodicals
Environmental sciences -- Research -- Periodicals
502.85 - Journal URLs:
- http://www.nature.com/ ↗
http://www.nature.com/srep/index.html ↗ - DOI:
- 10.1038/s41598-018-33647-w ↗
- Languages:
- English
- ISSNs:
- 2045-2322
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 10716.xml