Identification and functional analysis of cytochrome P450 complement in Streptomyces virginiaeIBL14

BMC Genomics

Research Article

Jie Yu¹  Man Li²  Li Xie²  Xiang Dong²  Wang-Yu Tong²  Xiao-Fei Li²  Zhi-Zhen Li²  Shu-Liang Zhu²  Wei Yang² 

[1] Department of Chemical Engineering, McMaster University, L8S 4L7, Hamilton, Ontario, Canada;Integrated Biotechnology Laboratory, Institute of Health Science, School of Life Science, Anhui University, 111 Jiulong Road, 230601, Hefei, China;

关键词: Biotransformation;    Cytochrome P450;    Ferredoxin;    Ferredoxin reductase;    Gene sequencing;    Secondary metabolism;   

DOI  :  10.1186/1471-2164-14-130

 received in 2012-10-25, accepted in 2013-02-21,  发布年份 2013

来源: Springer

【 摘 要 】

BackgroundAs well known, both natural and synthetic steroidal compounds are powerful endocrine disrupting compounds (EDCs) which can cause reproductive toxicity and affect cellular development in mammals and thus are generally regarded as serious contributors to water pollution. Streptomyces virginiae IBL14 is an effective degradative strain for many steroidal compounds and can also catalyze the C25 hydroxylation of diosgenin, the first-ever biotransformation found on the F-ring of diosgenin.ResultsTo completely elucidate the hydroxylation function of cytochrome P450 genes (CYPs) found during biotransformation of steroids by S. virginiae IBL14, the whole genome sequencing of this strain was carried out via 454 Sequencing Systems. The analytical results of BLASTP showed that the strain IBL14 contains 33 CYPs, 7 ferredoxins and 3 ferredoxin reductases in its 8.0 Mb linear chromosome. CYPs from S. virginiae IBL14 are phylogenetically closed to those of Streptomyces sp. Mg1 and Streptomyces sp. C. One new subfamily was found as per the fact that the CYP Svu001 in S. virginiae IBL14 shares 66% identity only to that (ZP_05001937, protein identifer) from Streptomyces sp. Mg1. Further analysis showed that among all of the 33 CYPs in S. virginiae IBL14, three CYPs are clustered with ferredoxins, one with ferredoxin and ferredoxin reductase and three CYPs with ATP/GTP binding proteins, four CYPs arranged with transcriptional regulatory genes and one CYP located on the upstream of an ATP-binding protein and transcriptional regulators as well as four CYPs associated with other functional genes involved in secondary metabolism and degradation.ConclusionsThese characteristics found in CYPs from S. virginiae IBL14 show that the EXXR motif in the K-helix is not absolutely conserved in CYP157 family and I-helix not absolutely essential for the CYP structure, too. Experimental results showed that both CYP Svh01 and CYP Svu022 are two hydroxylases, capable of bioconverting diosgenone into isonuatigenone and β-estradiol into estriol, respectively.

【 授权许可】

Unknown   
© Li et al; licensee BioMed Central Ltd. 2013. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.