A transport system for thymine was investigated in a Lactobacillus casei mutant lacking thymidine phosphorylase activity (the first enzyme required for thymine utilization). Transport was dependent on an energy supply; transport was inhibited by the uncouplers carbonylcyanide-m-chlorophenylhydrazone (CCCP) and 2,4 dinitrophenol (DNP), and also by sodium azide and N,N'-dicyclohexylcarbodiimide (DCCD). Thymine transport was inhibited by some uracil and adenosine derivatives and by thymidine, but was not affected by guanosine, deoxycytidine or azacytidine. Inhibition by p-chloromercurybenzoate (PCMB) was reversed by dithiothreitol (DTT).