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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
Nie, Yong ; Liang, Jieliang ; Fang, Hui ; Tang, Yue-Qin ; Wu, Xiao-Lei
刊名applied and environmental microbiology
2011
关键词COMPLETE GENOME SEQUENCE ELECTRON-TRANSFER COMPLEX PSEUDOMONAS-OLEOVORANS CRYSTAL-STRUCTURE ESCHERICHIA-COLI STRAIN IDENTIFICATION OXIDATION REDUCTASE MONOOXYGENASE
DOI10.1128/AEM.00203-11
英文摘要Two alkane hydroxylase-rubredoxin fusion gene homologs (alkW1 and alkW2) were cloned from a Dietzia strain, designated DQ12-45-1b, which can grow on crude oil and n-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 the alkW1 gene in DQ12-45-1b was induced when cells were grown on C(8) to C(32) n-alkanes as sole carbon sources, but expression of the alkW2 gene was not detected. Functional heterologous expression in an alkB deletion mutant of Pseudomonas fluorescens KOB2 Delta 1 suggested the alkW1 could restore the growth of KOB2 Delta 1 on C(14) and C(16) n-alkanes and induce faster growth on C(18) to C(32) n-alkanes than alkW1 Delta Rd, the Rd domain deletion mutant gene of alkW1, which also caused faster growth than KOB2 Delta 1 itself. In addition, the artificial fusion of AlkB from the Gram-negative P. fluorescens CHA0 and the Rds from both Gram-negative P. fluorescens CHA0 and Gram-positive Dietzia sp. DQ12-45-1b significantly increased the degradation of C(32) alkane compared to that seen with AlkB itself. In conclusion, the alkW1 gene cloned from Dietzia species encoded an alkane hydroxylase which increased growth on and degradation of n-alkanes up to C(32) 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-chain n-alkanes (such as C(32)) in the Gram-negative bacterium.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000295836700026&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biotechnology & Applied Microbiology; Microbiology; SCI(E); EI; PubMed; 21; ARTICLE; 20; 7279-7288; 77
语种英语
内容类型期刊论文
源URL[http://ir.pku.edu.cn/handle/20.500.11897/315688]  
专题工学院
推荐引用方式
GB/T 7714
Nie, Yong,Liang, Jieliang,Fang, Hui,et al. 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[J]. applied and environmental microbiology,2011.
APA Nie, Yong,Liang, Jieliang,Fang, Hui,Tang, Yue-Qin,&Wu, Xiao-Lei.(2011).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.applied and environmental microbiology.
MLA Nie, Yong,et al."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".applied and environmental microbiology (2011).
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