期刊
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
卷 79, 期 9, 页码 2882-2890出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.03980-12
关键词
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资金
- Agencia Nacional de Promocion Cientifica y Tecnologica of Argentina (ANPCyT) [PICT2010-1828, PICT 2008-1562]
- European Union [KBBE-211441]
- Boehringer Ingelheim Fonds Stiftung fur Medizinische Grundlagenforschung Euro Tango
Enterococcus faecalis encodes a biotin-dependent oxaloacetate decarboxylase (OAD), which is constituted by four subunits: E. faecalis carboxyltransferase subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and the novel subunit Ef-H. Our results show that in E. faecalis, subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex (termed Ef-AHD) which is also associated with the membrane. In order to characterize the role of the novel Ef-H subunit, coexpression of oad genes was performed in Escherichia coli, showing that this subunit is vital for Ef-A and Ef-D interaction. Diminished growth of the oadA and oadD single deletion mutants in citrate-supplemented medium indicated that the activity of the complex is essential for citrate utilization. Remarkably, the oadB-deficient strain was still capable of growing to wild-type levels but with a delay during the citrate-consuming phase, suggesting that the soluble Ef-AHD complex is functional in E. faecalis. These results suggest that the Ef-AHD complex is active in its soluble form, and that it is capable of interacting in a dynamic way with the membrane-bound Ef-B subunit to achieve its maximal alkalinization capacity during citrate fermentation.
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