LaoABCR, a novel system for oxidation of long-chain alcohols derived from SDS and alkane degradation in Pseudomonas aeruginosa.

Abstract

The opportunistic pathogen Pseudomonas aeruginosa strain PAO1 is able to use a variety of organic pollutants as growth substrates, including the anionic detergent sodium dodecyl sulfate (SDS) and long-chain alkanes. While the enzymes initiating SDS and alkane degradation are well known, the subsequent enzymatic steps for degradation of the derived primary long-chain alcohols have not yet been identified. By evaluating genes specifically induced during growth with SDS, a gene cluster encoding a putative alcohol dehydrogenase (PA0364/LaoA), a probable inner membrane protein (PA0365/ LaoB), and a presumable aldehyde dehydrogenase (PA0366/LaoC) was identified and designated the Lao (long-chain-alcohol/aldehyde-oxidation) system. Growth experiments with deletion mutants with SDS, 1-dodecanol, and alkanes revealed that LaoA and LaoB are involved in the degradation of primary long-chain alcohols. Moreover, detection of 1-dodecanol oxidation in cell extracts by activity staining revealed an interdependency of LaoA and LaoB for efficient 1-dodecanol oxidation. An in silico analysis yielded no well-characterized homologue proteins for LaoA and LaoB. Furthermore, a gene adjacent to the lao gene cluster encodes a putative transcriptional regulator (PA0367/LaoR). A laoR deletion mutant exhibited constitutive expression of LaoA and LaoB, indicating that LaoR is a repressor for the expression of laoABC. Taken together, these results showed that the proteins LaoA and LaoB constitute a novel oxidation system for long-chain alcohols derived from pollutants.