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荚膜红细菌 AnfA 对于 Fe-氮酶蛋白的合成是必需的，但对于辅因子生物合成和电子供应是可有可无的。

Rhodobacter capsulatus AnfA is essential for production of Fe-nitrogenase proteins but dispensable for cofactor biosynthesis and electron supply.

机构信息

Microbial Biology, Faculty of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany.

出版信息

Microbiologyopen. 2020 Jun;9(6):1234-1246. doi: 10.1002/mbo3.1033. Epub 2020 Mar 23.

DOI:10.1002/mbo3.1033
PMID:32207246
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7294313/
Abstract

The photosynthetic α-proteobacterium Rhodobacter capsulatus reduces and thereby fixes atmospheric dinitrogen (N ) by a molybdenum (Mo)-nitrogenase and an iron-only (Fe)-nitrogenase. Differential expression of the structural genes of Mo-nitrogenase (nifHDK) and Fe-nitrogenase (anfHDGK) is strictly controlled and activated by NifA and AnfA, respectively. In contrast to NifA-binding sites, AnfA-binding sites are poorly defined. Here, we identified two highly similar AnfA-binding sites in the R. capsulatus anfH promoter by studying the effects of promoter mutations on in vivo anfH expression and in vitro promoter binding by AnfA. Comparison of the experimentally determined R. capsulatus AnfA-binding sites and presumed AnfA-binding sites from other α-proteobacteria revealed a consensus sequence of dyad symmetry, TAC-N -GTA, suggesting that AnfA proteins bind their target promoters as dimers. Chromosomal replacement of the anfH promoter by the nifH promoter restored anfHDGK expression and Fe-nitrogenase activity in an R. capsulatus strain lacking AnfA suggesting that AnfA is required for AnfHDGK production, but dispensable for biosynthesis of the iron-only cofactor and electron delivery to Fe-nitrogenase, pathways activated by NifA. These observations strengthen our model, in which the Fe-nitrogenase system in R. capsulatus is largely integrated into the Mo-nitrogenase system.

摘要

光合 α-变形菌荚膜红细菌通过钼氮酶和铁氮酶还原并固定大气中的二氮 (N2)。Mo-氮酶（nifHDK）和 Fe-氮酶（anfHDGK）的结构基因的差异表达分别受到 NifA 和 AnfA 的严格控制和激活。与 NifA 结合位点不同，AnfA 结合位点的定义较差。在这里，我们通过研究启动子突变对体内 anfH 表达和体外 AnfA 结合的影响，在荚膜红细菌 anfH 启动子中鉴定了两个高度相似的 AnfA 结合位点。比较实验确定的荚膜红细菌 AnfA 结合位点和其他 α-变形菌的推定 AnfA 结合位点揭示了二联体对称性的保守序列 TAC-N-GTA，表明 AnfA 蛋白以二聚体结合其靶启动子。通过染色体替换，用 nifH 启动子替换 anfH 启动子，在缺乏 AnfA 的荚膜红细菌菌株中恢复了 anfHDGK 的表达和 Fe-氮酶活性，这表明 AnfA 是 AnfHDGK 产生所必需的，但对于铁单因子的生物合成和电子传递到 Fe-氮酶是可有可无的，这些途径是由 NifA 激活的。这些观察结果加强了我们的模型，即在荚膜红细菌中，Fe-氮酶系统在很大程度上整合到 Mo-氮酶系统中。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/abe6927635e7/MBO3-9-e1033-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/7536e139bc49/MBO3-9-e1033-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/dc7af2955ba4/MBO3-9-e1033-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/aaf64cecbc6f/MBO3-9-e1033-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/dcdb42536cdb/MBO3-9-e1033-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/1e70957c0e6d/MBO3-9-e1033-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/abe6927635e7/MBO3-9-e1033-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/7536e139bc49/MBO3-9-e1033-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/dc7af2955ba4/MBO3-9-e1033-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/aaf64cecbc6f/MBO3-9-e1033-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/dcdb42536cdb/MBO3-9-e1033-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/1e70957c0e6d/MBO3-9-e1033-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4ce6/7294313/abe6927635e7/MBO3-9-e1033-g006.jpg

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