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6. Formation of NifA-PIIcomplex represses ammonium-sensitive nitrogen fixation in diazotrophic proteobacteria lacking NifL

Author

Zeng, Yan, Guo, Lu, Gao, Yongqiang, Cui, Lingwei, Wang, Mengmei, Huang, Lu, Jiang, Mingyue, Liu, Ying, Zhu, Yaxin, Xiang, Hua, Li, De-Feng, and Zheng, Yanning

Abstract

Biological nitrogen fixation catalyzed by nitrogenase contributes greatly to the global nitrogen cycle. Nitrogenase expression is subject to regulation in response to nitrogen availability. However, the mechanism through which the transcriptional activator NifA regulates nitrogenase expression by interacting with PIInitrogen regulatory proteins remains unclear in diazotrophic proteobacteria lacking NifL. Here, we demonstrate that in Rhodopseudomonas palustrisgrown with ammonium, NifA bound deuridylylated PIIproteins to form an inactive NifA-PIIcomplex, thereby inhibiting the expression of nitrogenase. Upon nitrogen limitation, the dissociation of uridylylated PIIproteins from NifA resulted in the full restoration of NifA activity, and, simultaneously, uridylylation of the significantly up-regulated PIIprotein GlnK2 led to the increased expression of NifA in R. palustris. This insight into how NifA interacts with PIIproteins and controls nitrogenase expression sets the stage for creating highly efficient diazotrophs, reducing the need for energy-intensive chemical fertilizers and helping to diminish carbon emissions.

Published
2024
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7. [Enhanced heterologous expression of the cytochrome c from uncultured anaerobic methanotrophic archaea].

Author

Cui L, Fan X, and Zheng Y

Subjects
Anaerobiosis, Archaea metabolism, Heme metabolism, Cytochromes c genetics, Cytochromes c metabolism, Escherichia coli genetics, Escherichia coli metabolism
Abstract

Cytochrome c is a type of heme proteins that are widely distributed in living organisms. It consists of heme and apocytochrome c, and has potential applications in bioelectronics, biomedicine and pollutant degradation. However, heterologous overexpression of cytochrome c is still challenging. To date, expression of the cytochrome c from uncultured anaerobic methanotrophic archaea has not been reported, and nothing is known about the function of this cytochrome c. A his tagged cytochrome c was successfully expressed in E. coli by introducing a thrombin at the N-terminus of CytC4 and co-expressing CcmABCDEFGH, which is responsible for the maturation of cytochrome c. Shewanella oneidensis , which naturally has enzymes for cytochrome c maturation, was then used as a host to further increase the expression of CytC4. Indeed, a significantly higher expression of CytC4 was achieved in S. oneidensis when compared with in E. coli . The successful heterologous overexpression of CytC4 will facilitate the exploitation of its physiological functions and biotechnological applications.

Published
2022
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