Pyrimidine ribonucleoside degradation in the human pathogen Pseudomona
s aeruginosa ATCC 15692 was investigated. Either uracil, cytosine, 5-m
ethylcytosine, thymine, uridine or cytidine supported P. aeruginosa gr
owth as a nitrogen source when glucose served as the carbon source. Us
ing thin-layer chromatographic analysis, the enzymes nucleoside hydrol
ase and cytosine deaminase were shown to be active in ATCC 15692. Comp
ared to (NH4)(2)SO4-grown cells, nucleoside hydrolase activity in ATCC
15692 approximately doubled after growth on 5-methylcytosine as a nit
rogen source while its cytosine deaminase activity increased several-f
old after growth on the pyrimidine bases and ribonucleosides examined
as nitrogen sources. Regulation at the level of protein synthesis by 5
-methylcytosine was indicated for nucleoside hydrolase and cytosine de
aminase in P. aeruginosa.