Channelling of deoxyribose moiety of exogenous DNA into carbohydrate metabolism: role of deoxyriboaldolase.
In bacteria, the addition of (deoxy)nucleosides or (deoxy)ribose to the growth medium causes induction of enzymes involved in their catabolism, leading to the utilisation of the pentose moiety as carbon and energy source. In this respect, deoxyriboaldolase appears the key enzyme, allowing the utilisation of deoxyribose 5-P through glycolysis. We observed that not only deoxynucleosides, but also DNA added to the growth medium of Bacillus cereus induced deoxyriboaldolase; furthermore, the switch of the culture from aerobic to anaerobic conditions caused a further increase in enzyme activity, leading to a more efficient channelling of deoxyribose 5-P into glycolysis, probably as a response to the low energy yield of the sugar fermentation. In eukaryotes, the catabolism of (deoxy)nucleosides is well known. However, the research in this field has been mainly devoted to the salvage of the bases formed by the action of nucleoside phosphorylases, whereas the metabolic fate of the sugar moiety has been largely neglected. Our results indicate that the deoxyriboaldolase activity is present in the liver of several vertebrates and in a number of cell lines. We discuss our observations looking at the nucleic acids not only as informational molecules, but also as a not negligible source of readily usable phosphorylated sugar.
Sgarrella
F
F
Dipartimento di Scienze del Farmaco, Università di Sassari, Italy.
Poddie
F P
FP
Meloni
M A
MA
Sciola
L
L
Pippia
P
P
Tozzi
M G
MG
D000446:Aldehyde-Lyases / Q000378:metabolism*; D000650:Amnion; D000818:Animals; D001409:Bacillus cereus / Q000201:enzymology* / Q000254:growth & development; D050260:Carbohydrate Metabolism; D002460:Cell Line; D004247:DNA / Q000378:metabolism*; D003855:Deoxyribose / Q000378:metabolism*; D005285:Fermentation; D006019:Glycolysis; D006801:Humans; D008099:Liver / Q000201:enzymology
D003855:Deoxyribose; D004247:DNA; D000446:Aldehyde-Lyases; C020019:deoxyribose-phosphate aldolase