DNA fragments containing the xylD and xylL genes of TOL plasmid pWW0-161 of Pseudomonas putida, which code for the catabolic enzymes toluate 1,2-dioxygenase and dihydrodihydroxybenzoic acid dehydrogenase, respectively, and the nahG gene of the NAH plasmid NAH7, which codes for salicylate hydroxylase, were cloned in pBR322 vector plasmid. Deletion and insertion mutagenesis were used to localize these genes with respect to crucial endonuclease cleavage sites. The pBR322-based plasmids were ligated to the broad host range cloning vector pKT231, or derivatives of it, and the hybrid plasmids were introduced into Pseudomonas sp. B13(WR1), a bacterium able to degrade 3-chlorobenzoate but not 4chlorobenzoate, 3,5-dichlorobenzoate, salicylate, or chlorosalicylates. The cloned xylD gene expanded the catabolic range of WRl to include 4-chlQrobenzoate, whereas the cloned xylD-xylL genes enabled the isolation of derivatives of WRl that degraded 3-chlorobenzoate, 4-chlorobenzoate, and 3,5-dichlorobenzoate. The cloned nahG gene extended the catabolic range of WRl to include salicylate and 3-, 4-, and 5-chlorosalicylate.