The Disruption of an OxyR-Like Protein Impairs Intracellular Magnetite Biomineralization in Magnetospirillum gryphiswaldense MSR-1
文献类型: 外文期刊
第一作者: Zhang, Yunpeng
作者: Zhang, Yunpeng;Wen, Tong;Guo, Fangfang;Geng, Yuanyuan;Liu, Junquan;Peng, Tao;Guan, Guohua;Tian, Jiesheng;Li, Ying;Li, Jilun;Jiang, Wei;Zhang, Yunpeng;Wen, Tong;Guo, Fangfang;Geng, Yuanyuan;Liu, Junquan;Peng, Tao;Guan, Guohua;Tian, Jiesheng;Li, Ying;Li, Jilun;Jiang, Wei;Zhang, Yunpeng;Wen, Tong;Geng, Yuanyuan;Liu, Junquan;Guan, Guohua;Tian, Jiesheng;Li, Ying;Li, Jilun;Jiang, Wei;Guo, Fangfang;Ju, Jing
作者机构:
关键词: OxyR-like protein; magnetosome formation; Magnetospirillum gryphiswaldense MSR-1; carbon metabolism; biomineralization
期刊名称:FRONTIERS IN MICROBIOLOGY ( 影响因子:5.64; 五年影响因子:6.32 )
ISSN: 1664-302X
年卷期: 2017 年 8 卷
页码:
收录情况: SCI
摘要: Magnetotactic bacteria synthesize intracellular membrane-enveloped magnetite bodies known as magnetosomes which have been applied in biotechnology and medicine. A series of proteins involved in ferric ion transport and redox required for magnetite formation have been identified but the knowledge of magnetosome biomineralization remains very limited. Here, we identify a novel OxyR homolog (named OxyR-Like), the disruption of which resulted in low ferromagnetism and disfigured nano-sized iron oxide crystals. High resolution-transmission electron microscopy showed that these nanoparticles are mainly composed of magnetite accompanied with ferric oxide including a-Fe2O3 and +-Fe2O3. Electrophoretic mobility shift assay and DNase I footprinting showed that OxyR-Like binds the conserved 5'-GATA-N{9}-TATC-3' region within the promoter of pyruvate dehydrogenase (pdh) complex operon. Quantitative real-time reverse transcriptase PCR indicated that not only the expression of pdh operon but also genes related to magnetosomes biosynthesis and tricarboxylic acid cycle decreased dramatically, suggesting a link between carbon metabolism and magnetosome formation. Taken together, our results show that OxyR-Like plays a key role in magnetosomes formation.
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