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<p>The symbiotic nitrogen-fixing bacterium <i>Bradyrhizobium japonicum</i> (<i>B.japonicum</i>) enables high soybean yields with little or no nitrogen fertiliser. A two component regulatory system comprising FixL, a histidine kinase with O<sub>2</sub>-sensing activity, and FixJ, a response regulator, controls the expression of genes involved in nitrogen fixation, such as <i>fixK</i> and <i>nifA</i>. Only under anaerobic conditions, the monophosphate group is transferred from FixL to the N-terminal receiver domain of FixJ (FixJ<sub>N</sub>), which eventually promote the association of the C-terminal effector domain (FixJ<sub>C</sub>) to the promoter regions of the nitrogen-fixation-related genes. Structural biological analyses carried out so far for rhizobial FixJ molecules have proposed a solution structure for FixJ that differs from the crystal structures, in which the two domains are extended. To understand the FixJ activation caused by phosphorylation of the N-terminal domain, which presumably regulates through the interactions between FixJ<sub>N</sub> and FixJ<sub>C</sub>, here we have performed backbone and sidechain resonance assignments of the unphosphorylated state of <i>B. japonicum</i> FixJ.</p>

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Backbone and side‑chain 1H, 13C and 15N resonance assignments and secondary structure determination of the rhizobial FixJ

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年2月1日

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  • Akio Horikawa,
  • Rika Okubo,
  • Naoki Hishikura,
  • Riki Watanabe,
  • Kaori Kurashima-Ito,
  • Pooppadi Maxin Sayeesh,
  • Kohsuke Inomata,
  • Masaki Mishima,
  • Hiroyasu Koteishi,
  • Hitomi Sawai,
  • Yoshitsugu Shiro,
  • Teppei Ikeya,
  • Yutaka Ito

摘要

The symbiotic nitrogen-fixing bacterium Bradyrhizobium japonicum (B.japonicum) enables high soybean yields with little or no nitrogen fertiliser. A two component regulatory system comprising FixL, a histidine kinase with O2-sensing activity, and FixJ, a response regulator, controls the expression of genes involved in nitrogen fixation, such as fixK and nifA. Only under anaerobic conditions, the monophosphate group is transferred from FixL to the N-terminal receiver domain of FixJ (FixJN), which eventually promote the association of the C-terminal effector domain (FixJC) to the promoter regions of the nitrogen-fixation-related genes. Structural biological analyses carried out so far for rhizobial FixJ molecules have proposed a solution structure for FixJ that differs from the crystal structures, in which the two domains are extended. To understand the FixJ activation caused by phosphorylation of the N-terminal domain, which presumably regulates through the interactions between FixJN and FixJC, here we have performed backbone and sidechain resonance assignments of the unphosphorylated state of B. japonicum FixJ.