Advanced Analysis Center, National Agriculture and Food Research Organization (NAAC/NARO), Tsukuba, Ibaraki, Japan.
Food Research Institute, National Agriculture and Food Research Organization (NFRI/NARO), Tsukuba, Ibaraki, Japan.
Biosci Biotechnol Biochem. 2021 Feb 18;85(2):297-306. doi: 10.1093/bbb/zbaa037.
Bacillus subtilis YabJ protein belongs to the highly conserved YjgF/YER057c/UK114 family, which has a homotrimeric quaternary structure. The dominant allele of yabJ gene that is caused by a single amino acid mutation of Ser103Phe enables poly-γ-glutamic acid (γPGA) production of B. subtilis under conditions where the cell-density signal transduction was disturbed by the loss of DegQ function. X-ray crystallography of recombinant proteins revealed that unlike the homotrimeric wild-type YabJ, the mutant YabJ(Ser103Phe) had a homotetrameric quaternary structure, and the structural change appeared to be triggered by an inversion of the fifth β-strand. The YabJ homotetramer has a hole that is highly accessible, penetrating through the tetramer, and 2 surface concaves as potential ligand-binding sites. Western blot analyses revealed that the conformational change was also induced in vivo by the Ser103Phe mutation.
枯草芽孢杆菌 YabJ 蛋白属于高度保守的 YjgF/YER057c/UK114 家族，具有三聚体四级结构。yabJ 基因的优势等位基因是由于丝氨酸 103 突变为苯丙氨酸，使得枯草芽孢杆菌能够在 DegQ 功能丧失导致细胞密度信号转导受到干扰的情况下产生聚-γ-谷氨酸（γPGA）。重组蛋白的 X 射线晶体学表明，与三聚体野生型 YabJ 不同，突变体 YabJ（Ser103Phe）具有四聚体同源结构，结构变化似乎是由第五个β-链的反转引发的。YabJ 四聚体有一个高度可及的孔，贯穿四聚体，2 个表面凹痕作为潜在的配体结合位点。Western blot 分析表明，该构象变化也由 Ser103Phe 突变在体内诱导。
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