2024-10-082024-10-082018-10-192045-2322https://hdl.handle.net/2133/27942ADP-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 species Escherichia 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 the E. 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 identifed during screening lacked functions that underlie envelope biogenesis and integrity, including the RpoE specifc 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 that E. 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.1-15enopenAccessEscherichia coliAdenine nucleotidesAdenosine diphosphate glucoseNucleoside transport proteinsStress physiologiqueAdenosine diphosphatearticuloAlmagro, GoizederViale, Alejandro M.Montero, ManuelMuñoz, Francisco JoséBaroja Fernández, EdurneMori, HirotadaPozueta Romero, JavierUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y FarmacéuticasAttribution 4.0 International