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Two alkane hydroxylase-rubredoxin fusion gene homologs (alkW1 andalkW2 ) were cloned from aDietzia strain, designated DQ12-45-1b, which can grow on crude oil andn -alkanes ranging in length from 6 to 40 carbon atoms as sole carbon sources. Both AlkW1 and AlkW2 have an integral-membrane alkane monooxygenase (AlkB) conserved domain and a rubredoxin (Rd) conserved domain which are fused together. Phylogenetic analysis showed that these two AlkB-fused Rd domains formed a novel third cluster with all the Rds from the alkane hydroxylase-rubredoxin fusion gene clusters in Gram-positive bacteria and that this third cluster was distant from the known AlkG1- and AlkG2-type Rds. Expression of thealkW1 gene in DQ12-45-1b was induced when cells were grown on C8 to C32 n -alkanes as sole carbon sources, but expression of thealkW2 gene was not detected. Functional heterologous expression in analkB deletion mutant ofPseudomonas fluorescens KOB2Δ1 suggested thealkW1 could restore the growth of KOB2Δ1 on C14 and C16 n -alkanes and induce faster growth on C18 to C32 n -alkanes thanalkW1 ΔRd, the Rd domain deletion mutant gene ofalkW1 , which also caused faster growth than KOB2Δ1 itself. In addition, the artificial fusion of AlkB from the Gram-negativeP. fluorescens CHA0 and the Rds from both Gram-negativeP. fluorescens CHA0 and Gram-positiveDietzia sp. DQ12-45-1b significantly increased the degradation of C32 alkane compared to that seen with AlkB itself. In conclusion, thealkW1 gene cloned fromDietzia species encoded an alkane hydroxylase which increased growth on and degradation ofn -alkanes up to C32 in length, with its fused rubredoxin domain being necessary to maintain the functions. In addition, the fusion of alkane hydroxylase and rubredoxin genes from both Gram-positive and -negative bacteria can increase the degradation of long-chainn -alkanes (such as C32 ) in the Gram-negative bacterium.

applied and environmental microbiology

Two Novel Alkane Hydroxylase-Rubredoxin Fusion Genes Isolated from a Dietzia Bacterium and the Functions of Fused Rubredoxin Domains in Long-Chain <i>n</i> -Alkane Degradation

Two Novel Alkane Hydroxylase-Rubredoxin Fusion Genes Isolated from a Dietzia Bacterium and the Functions of Fused Rubredoxin Domains in Long-Chain n -Alkane Degradation