Open AccessTetramer formation of Bacillus subtilis YabJ protein that belongs to YjgF/YER057c/UK114 family
Author(s) -
Zui Fujimoto,
Le Hong,
N. Kishine,
Nobuhiro Suzuki,
Keitarou Kimura
Publication year - 2021
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1093/bbb/zbaa037
Subject(s) - homotetramer , bacillus subtilis , tetramer , mutant , protein quaternary structure , chemistry , recombinant dna , amino acid , mutation , protein structure , biology , microbiology and biotechnology , biochemistry , gene , genetics , enzyme , protein subunit , bacteria
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.
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